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Literature summary for 2.4.1.B64 extracted from

  • Liebau, J.; Fu, B.; Brown, C.; Maeler, L.
    New insights into the membrane association mechanism of the glycosyltransferase WaaG from Escherichia coli (2018), Biochim. Biophys. Acta, 1860, 683-690 .
    View publication on PubMed
Search for more literature for 2.4.1.B64

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-AI Escherichia coli

Protein Variants

Protein Variants Comment Organism
F322W site-directed mutagenesis, analysis of the lipid binsing compared to wild-type enzyme Escherichia coli
Y115W site-directed mutagenesis, analysis of the lipid binsing compared to wild-type enzyme Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane WaaG is membrane-bound, membrane association mechanism, overview. Binding of WaaG to membranes is analyzed by stopped-flow fluorescence and NMR diffusion experiments. Electrostatic interactions are required to bind WaaG to membranes while mere hydrophobic interactions are not sufficient. WaaG senses the membrane's surface charge density but there is no preferential binding to specific anionic lipids. The binding is weaker than expected for monotopic GTs but similar to peripheral GTs. Therefore, WaaG may be a peripheral GT and this can be of functional relevance in vivo since LPS synthesis occurs only when WaaG is membrane-bound. No C-terminal domain movement is observed under the experimental conditions Escherichia coli 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli P25740
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-AI by nickel affinity chromatography and dialysis Escherichia coli

Synonyms

Synonyms Comment Organism
glycosyltransferase WaaG
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 Escherichia coli
WaaG
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 Escherichia coli

General Information

General Information Comment Organism
additional information retaining GTs show a front-face catalytic mechanism. Glycosyltransferases GTs constitute a diverse class of enzymes that catalyze the formation of glycosidic bonds. GTs are highly versatile as they catalyze the transfer of sugar moieties from activated donor molecules to a vast amount of acceptor molecules but are at the same time highly specific for donor and acceptor molecules Escherichia coli
physiological function glycosyltransferase WaaG is involved in the synthesis of lipopolysaccharides (LPS) in Gram-negative bacteria and is previously categorized as a monotopic glycosyltransferase (GT). Membrane-associated GTs have the peculiar property that they catalyze the formation of a glycosidic bond between a hydrophilic donor substrate and a lipid acceptor molecule. Moreover, peripheral GTs can either be membrane-bound or soluble. WaaG binds membranes via electrostatic interactions. There is no specific binding to anionic lipids. WaaG senses the anionic surface charge density of the membrane. The N- and C-terminal domains both associate to the lipid membrane with similar changes in fluorescence properties of a reporter Trp residue positioned in either the N-terminal or C-terminal domain. WaaG is a peripheral membrane protein Escherichia coli