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(bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
-
-
-
-
?
(GalNAc2-bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
-
-
-
-
?
(Glc1GalNAc5-bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
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-
-
-
?
Lys-Asp-Phe-Asn-Val-Ser-Lys-Ala + N-acetyl-alpha-D-galactosaminyl-diphospho-tritrans,heptacis-undecaprenol
tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-beta-D-galactosaminyl]-Asn-Val-Ser-Lys-Ala
-
a chemically synthesized sugar donor with synthesized peptide acceptor
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-
?
N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol + KDFNVSKA
tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-beta-D-bacillosaminyl]-Asn-Val-Ser-Lys-Ala
-
oligosaccharyl transferase activity of PglB in vitro with synthetic disaccharide glycan donor and peptide acceptor substrate
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-
?
tritrans,heptacis-undecaprenyl diphospho-O1 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O1 antigen
-
from Shigella dysenteriae
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O11 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O11 antigen
-
from Pseudomonas aeruginosa
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O157 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O157 antigen
-
from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O16 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O16 antigen
-
from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O7 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O7 antigen
-
from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O9 antigen + [Acra]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [Acra]-L-asparagine-O9 antigen
-
PglB transfers the O9a antigen, an ABC transporter-dependent O antigen, to AcrA in Escherichia coli strain CWG28, the K30 antigen is not transferred to AcrA
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [HmcA]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [HmcA]-L-asparagine-oligosaccharide
-
a protein from Desulfovibrio gigas, N-glycosylation site is N261
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
additional information
?
-
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
-
-
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
a conserved DGGK motif is essential for the function of the PglB oligosaccharyltransferase
-
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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the native substrate for PglB is a heptasaccharide
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
as glycoprotein targets are used Escherichia coli maltose binding protein which is a native periplasmic protein and the anti-beta-galactosidase single-chain antibody fragment called scFv13-R4 that is modified with an N-terminal cotranslational export signal from Escherichia coli DsbA. The proteins are each modified C-terminally with four tandem repeats of the bacterial glycan acceptor motif DQNAT and recombinantly expressed, overview
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
i.e. substrate peptide LLO, modelling of active site binding, overview, and glycosylation acceptor protein 3D5, a single-chain Fv fragment containing aDQNATacceptor sequon
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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transfer of an oligosaccharide from a polyisoprenyl pyrophosphate carrier to the asparagine side chain of proteins within the conserved glycosylation sites D/E-X1-N-X2-S/T, where X1 and X2 can be any amino acids except proline, sequence DQNAT is the optimal acceptor substrate
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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as glycoprotein targets are used Escherichia coli maltose binding protein which is a native periplasmic protein and the anti-beta-galactosidase single-chain antibody fragment called scFv13-R4 that is modified with an N-terminal cotranslational export signal from Escherichia coli DsbA. The proteins are each modified C-terminally with four tandem repeats of the bacterial glycan acceptor motif DQNAT and recombinantly expressed, overview
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
i.e. substrate peptide LLO, modelling of active site binding, overview, and glycosylation acceptor protein 3D5, a single-chain Fv fragment containing a DQNAT acceptor sequon
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
PglBDd can transfer mono- and polysaccharides. LLO and AcrA and substrate glycosylation sites, overview. PglBDd does not require a negatively charged residue in the -2 position of the glycosylation sequon N-X-S/T
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
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-
?
additional information
?
-
-
PglBCj can glycosylate residues in both unstructured and structured regions of eukaryotic acceptor proteins in vivo
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-
?
additional information
?
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ability of PglB to transfer a wide variety of saccharides and peptides, substrate specificity, mass spectrometric glycopeptide product analysis, overview. PglB readily accepts a disaccharide in vitro. PglB does require determinants in the peptide sequence beyond the canonical N-X-S/Ttripeptide
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-
?
additional information
?
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-
peptide substrate library construction, based on the known glycosylation site 88DFNVS92 from the Campylobacter jejuni glycoprotein PEB3, and assessment of the amino acids at each position of the consensus glycosylation sequence for their impact on glycosylation efficiency using a quantitative radioactivity-based in vitro assay, and glycosylation sequences specificity, overview. Circular dichroism spectra of acceptor proteins. PglB is inactive with glycosyl donors such as dolichyl-pyrophosphatechitobiose
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-
?
additional information
?
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-
PglB is solely responsible for the oligosaccharyltransferase activity, PglB exhibits relaxed sugar substrate specificity
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-
?
additional information
?
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PglB-dependent N-glycosylation, structural analysis of in vitro-generated glycopeptides, overview
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-
?
additional information
?
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PglBCj adds two glycan chains to model protein acceptor AcrA. PglBCj recognizes the conventional bacterial glycosylation sequon consisting of the sequence D/E-X1-NNX2-S/T, where X1 and X2 are any amino acid except proline, in contrast to PglBDd from Desulfovibrio desulfuricans, overview. AcrA contains five potential N-glycosylation sites N-X-S/T, but only the two that have an Asp residue at the -2 position are recognized by the Campylobacter jejuni enzyme, N123 and N273
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-
?
additional information
?
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-
PglBCj is able to transfer Man3GlcNAc2 to extended sites but not to minimal glycosylation sites in engineered or eukaryotic target proteins
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-
?
additional information
?
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-
the PglB relaxed oligosaccharide substrate specificity allows the transfer of different glycans from the lipid carrier undecaprenyl pyrophosphate to an acceptor protein, substrate specificity of PglB with a set of lipid-linked polysaccharides in Escherichia coli and Salmonella enterica serovar Typhimurium. PglB required an acetamido group at the C-2, while a hexose linked to the C-6 of the monosaccharide at the reducing end does not inhibit the transfer of the O antigen to the acceptor protein, mechanism of PglB, modeling, overview. The Salmonella enterica O antigen containing Gal at the reducing end , and K30 capsular antigen, and LT2 antigen are not substrates for PglB, as
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-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglB-dependent N-glycosylation, structural analysis of in vitro-generated glycopeptides, overview
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-
?
additional information
?
-
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PglBCl is able to transfer Man3GlcNAc2 to extended sites but not to minimal glycosylation sites in engineered or eukaryotic target proteins
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-
?
additional information
?
-
-
the recombinantly expressed PglB can transfer the Campylobacter jejuni heptasaccharide onto the model protein acceptor AcrA, PglBDd adds a single glycan chain to AcrA. PglBDd does not recognize the conventional bacterial glycosylation sequon consisting of the sequence D/E-X1-NNX2-S/T, where X1 and X2 are any amino acid except proline, and instead uses a different site for the attachment of the oligosaccharide than PglBCj from Campylobacter jejuni, PglBDd exhibits relaxed glycan specificity, being able to transfer mono- and polysaccharides to AcrA, overview
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-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglB1-dependent N glycosylation with a linear pentasaccharide requiring an acidic residue at the -2 position of the N-glycosylation sequon, structural analysis of in vitro-generated glycopeptides, overview
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-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglB1-dependent N glycosylation with a linear pentasaccharide requiring an acidic residue at the -2 position of the N-glycosylation sequon, structural analysis of in vitro-generated glycopeptides, overview
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-
?
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tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
-
-
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
additional information
?
-
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
the native substrate for PglB is a heptasaccharide
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglBCj can glycosylate residues in both unstructured and structured regions of eukaryotic acceptor proteins in vivo
-
-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
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evolution
bacterial PglB and archaeal AglB constitute a protein family of the catalytic subunit of OST, along with STT3 from eukaryotes, that has three types of OST catalytic centers, structure analysis and comparison, overview
evolution
-
eukaryotic and prokaryotic OTases catalyze the transfer of oligosaccharides by a conserved mechanism
evolution
-
in the delta proteobacteria Desulfovibrio sp., the PglB homologue is more closely related to eukaryotic and archaeal OTases than to its Campylobacter counterparts
evolution
-
sequence analysis using 28 homologs from evolutionarily distant organisms, relationship between PglB and other Stt3 proteins, detailed overview Several inter-transmembrane loop regions of PglB/Stt3 contain strictly conserved motifs that are essential for PglB function
evolution
-
bacterial PglB and archaeal AglB constitute a protein family of the catalytic subunit of OST, along with STT3 from eukaryotes, that has three types of OST catalytic centers, structure analysis and comparison, overview
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malfunction
-
if the WWDYGY signature sequence is mutated to WAAYGY, PglB is no longer active in vivo
malfunction
-
insertional knockout mutagenesis of the gene pglB2 is unsuccessful, suggesting that it is essential
malfunction
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insertional knockout mutagenesis of the gene pglB2 is unsuccessful, suggesting that it is essential
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metabolism
-
PglB is involved in the Campylobacter jejuni general N-linked protein glycosylation pathway, overview
metabolism
-
PglB is involved in the general N-linked glycosylation pathway encoded by the pgl gene cluster
metabolism
-
the central enzyme in N-linked glycosylation is the oligosaccharyl transferase PglB, which catalyzes glycan transfer from a polyprenyldiphosphate-linked carrier to select asparagines within acceptor proteins
physiological function
-
PglB catalyzes the transfer of an oligosaccharide from a polyisoprenyl pyrophosphate carrier to the asparagine side chain of proteins within the conserved glycosylation sites D/E-X1-N-X2-S/T, where X1 and X2 can be any amino acids except proline
physiological function
-
PglB catalyzes the transfer of an undecaprenyl-linked heptasaccharide to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif
physiological function
-
the central enzyme in N-linked glycosylation is the oligosaccharyl transferase PglB, which catalyzes glycan transfer from a polyprenyldiphosphate-linked carrier to select asparagines within acceptor proteins. Role of the intertransmembrane domain loops in OTase catalysis
physiological function
-
the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB
physiological function
-
the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB
physiological function
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
physiological function
-
the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB
-
physiological function
-
the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB
-
physiological function
-
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
-
additional information
-
several inter-transmembrane loop regions of PglB/Stt3 contain strictly conserved motifs that are essential for PglB function, these loops play a fundamental role in catalysis
additional information
-
structure-function relationships for the periplasmic domain of the N-oligosaccharyltransferase PglB, overview
additional information
-
the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
additional information
the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
additional information
-
the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
additional information
the PglB structure reveals a distinct catalytic motif in the transmembrane region that contributes to the catalytic function, structure analysis, overview
additional information
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topology mapping of PglB using the PhoA/LacZ fusion method, overview. The topological model shows that PglB possesses 11 transmembrane segments and two relatively large periplasmic regions other than the C-terminal domain, which is consistent with the proposal of the common Ncyt-Cperi topology with 11 transmembrane segments for the STT3 family proteins
additional information
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the PglB structure reveals a distinct catalytic motif in the transmembrane region that contributes to the catalytic function, structure analysis, overview
-
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Glover, K.J.; Weerapana, E.; Numao, S.; Imperiali, B.
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Campylobacter jejuni
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Campylobacter jejuni
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Campylobacter jejuni, Helicobacter pullorum, Helicobacter pullorum NCTC 12824, Campylobacter jejuni NCTC 11168
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Campylobacter jejuni
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Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases
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Campylobacter jejuni
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Campylobacter jejuni
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Ielmini, M.V.; Feldman, M.F.
Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements
Glycobiology
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2011
Campylobacter jejuni, Desulfovibrio desulfuricans
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Valderrama-Rincon, J.D.; Fisher, A.C.; Merritt, J.H.; Fan, Y.Y.; Reading, C.A.; Chhiba, K.; Heiss, C.; Azadi, P.; Aebi, M.; DeLisa, M.P.
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2012
Campylobacter jejuni, Campylobacter lari
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X-ray structure of a bacterial oligosaccharyltransferase
Nature
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2011
Campylobacter jejuni, Campylobacter lari (B9KDD4), Campylobacter lari
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Ishiwata, A.; Taguchi, Y.; Lee, Y.J.; Watanabe, T.; Kohda, D.; Ito, Y.
N-Glycosylation with synthetic undecaprenyl pyrophosphate-linked oligosaccharide to oligopeptides by PglB oligosaccharyltransferase from Campylobacter jejuni
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2015
Campylobacter jejuni
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Mohanty, S.; Chaudhary, B.P.; Zoetewey, D.
Structural insight into the mechanism of N-linked glycosylation by oligosaccharyltransferase
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Campylobacter lari (B9KDD4), Campylobacter lari RM2100 (B9KDD4)
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Barre, Y.; Nothaft, H.; Thomas, C.; Liu, X.; Li, J.; Ng, K.K.S.; Szymanski, C.M.
A conserved DGGK motif is essential for the function of the PglB oligosaccharyltransferase from Campylobacter jejuni
Glycobiology
27
978-989
2017
Campylobacter jejuni
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