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x * 30000, SDS-PAGE
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x * 30000, SDS-PAGE
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x * 31691, recombinant AroE, mass spectrometry
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x * 27200, SDS-PAGE
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?
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x * 50000-60000, recombinant enzyme, SDS-PAGE
dimer
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dimer
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2 * 32000, SDS-PAGE, 2 * 29140, deduced from gene sequence
dimer
2 * 30202, calculated
dimer
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2 * 30202, calculated
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dimer
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2 * 30000, native PAGE
dimer
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2 * 30000, native PAGE
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dimer
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recombinant paralogue HI0607, SDS-PAGE and gel filtration
dimer
2 * 54150, recombinant AroE, mass spectrometry
dimer
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2 * 54150, recombinant AroE, mass spectrometry
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monomer
in solution
monomer
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1 * 32000, SDS-PAGE
monomer
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1 * 29400, mass spectrometry and gel filtration
monomer
-
1 * 29414, mass spectrometry
monomer
-
1 * 30000, native PAGE
monomer
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1 * 30000, native PAGE
-
monomer
1 * 27000, recombinant AroE, SDS-PAGE, 1 * 27076, recombinant AroE, mass spectrometry
monomer
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1 * 27000, recombinant AroE, SDS-PAGE, 1 * 27076, recombinant AroE, mass spectrometry
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monomer
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1 * 29000, SDS-PAGE
monomer
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1 * 29000, SDS-PAGE
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monomer
1 * 28889, calculated
monomer
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1 * 28889, calculated
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additional information
SDH enzymes exist in opened and closed conformational states. In the ternary structure of Aquifex aeolicus SDH (PDB ID 2HK9), three loops in the shikimate binding domain are shifted about 5 A toward the NADP++ binding site compared to their position in an unliganded structure of the same enzyme (PDB ID 2HK8). The closed form of the structure thus brings the bound shikimate and NADP+ molecules into close proximity, facilitating a hydride transfer between the shikimate C5-hydroxyl and C4 of the NADP+ nicotinamide ring
additional information
the SDH domain is connected via its N-terminus to the DHQ module
additional information
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structure analysis, dynamic light scattering measurements
additional information
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three-dimensional structure analysis of AroE
additional information
three-dimensional structure analysis of AroE
additional information
analysis of secondary structure
additional information
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analysis of secondary structure
additional information
the active subpocket 1 is formed by residues Val8, Ser16, Ser18, Asn63, Val64, Thr65, Lys69, Asn90, Asp105, and Gln237, subpocket 2 by residues Asp105, Ser129, Ala179, Thr180, Ser181, Leu184, Leu208, Tyr210, Gly230, Met233, and Leu234, and subpocket 3 by residues Gly125, Ala126, Gly127, Asn148, Arg149, Ser150, Thr180, Ser181, Ala182, and Pro189
additional information
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the active subpocket 1 is formed by residues Val8, Ser16, Ser18, Asn63, Val64, Thr65, Lys69, Asn90, Asp105, and Gln237, subpocket 2 by residues Asp105, Ser129, Ala179, Thr180, Ser181, Leu184, Leu208, Tyr210, Gly230, Met233, and Leu234, and subpocket 3 by residues Gly125, Ala126, Gly127, Asn148, Arg149, Ser150, Thr180, Ser181, Ala182, and Pro189
additional information
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analysis of secondary structure
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additional information
the enzyme shows an alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively, a phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site, the structure reveals a topologically unique domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization, homology modeling, overview
additional information
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the enzyme shows an alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively, a phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site, the structure reveals a topologically unique domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization, homology modeling, overview
additional information
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the structure reveals an enzyme with a deep cleft, which contains the active site, formed at the junction of two domains. The C-terminal domain is easily recognizable as a Rossmann fold dinucleotide binding domain, responsible for binding the NADP cofactor. The N-terminal substrate binding and dimerization domain, an alpha-beta-alpha sandwich, represents a unique topological fold, structure modeling
additional information
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secondary structure analysis of ARoE, percentages for alpha-helix, beta-sheet, beta-turn, and random coil are 29.2%, 9.3%, 32.7%, and 28.8%, respectively, contains the highly conserved motif G-X-(N/S)-V-(T/S)-X-PX-K
additional information
three-dimensional structure analysis of wild-type and mutant enzymes with bound substrates, overview
additional information
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three-dimensional structure analysis of wild-type and mutant enzymes with bound substrates, overview
additional information
the overall structure of SDH comprises two alpha/beta domains linked centrally by two alpha-helices. A deep groove between these two domains contains the active site for the binding of substrate and cofactor
additional information
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the overall structure of SDH comprises two alpha/beta domains linked centrally by two alpha-helices. A deep groove between these two domains contains the active site for the binding of substrate and cofactor
additional information
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the DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
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the DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
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additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
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additional information
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three-dimensional structure determination by homology modelling and validation
additional information
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three-dimensional structure determination by homology modelling and validation
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additional information
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structural modeling of TgSDH suggests that the protein's three large amino acid insertions form surface-exposed loops with alpha-helical character, structure modelling and structure comparisons, overview