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| - | [[Image:1iir.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1iir| PDB=1iir | SCENE= }} | | {{STRUCTURE_1iir| PDB=1iir | SCENE= }} |
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| - | '''Crystal Structure of UDP-glucosyltransferase GtfB'''
| + | ===Crystal Structure of UDP-glucosyltransferase GtfB=== |
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| - | ==Overview==
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| - | BACKGROUND: Members of the vancomycin group of glycopeptide antibiotics have an oxidatively crosslinked heptapeptide scaffold decorated at the hydroxyl groups of 4-OH-Phegly4 or beta-OH-Tyr6 with mono- (residue 6) or disaccharides (residue 4). The disaccharide in vancomycin itself is L-vancosamine-1,2-glucose, and in chloroeremomycin it is L-4-epi-vancosamine-1,2-glucose. The sugars and their substituents play an important role in efficacy, particularly against vancomycin-resistant pathogenic enterococci. RESULTS: The glucosyltransferase, GtfB, that transfers the glucose residue from UDP-glucose to the 4-OH-Phegly4 residue of the vancomycin aglycone, initiating the glycosylation pathway in chloroeremomycin maturation, has been crystallized, and its structure has been determined by X-ray analysis at 1.8 A resolution. The enzyme has a two-domain structure, with a deep interdomain cleft identified as the likely site of UDP-glucose binding. A hydrophobic patch on the surface of the N-terminal domain is proposed to be the binding site of the aglycone substrate. Mutagenesis has revealed Asp332 as the best candidate for the general base in the glucosyltransfer reaction. CONCLUSIONS: The structure of GtfB places it in a growing group of glycosyltransferases, including Escherichia coli MurG and a beta-glucosyltransferase from T4 phage, which together form a subclass of the glycosyltransferase superfamily and give insights into the recognition of the NDP-sugar and aglycone cosubstrates. A single major interdomain linker between the N- and C- terminal domains suggests that reprogramming of sugar transfer or aglycone recognition in the antibiotic glycosyltransferases, including the glycopeptide and also the macrolide antibiotics, will be facilitated by this structural information.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11470430}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11470430 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11470430}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Glycosyltransferase]] | | [[Category: Glycosyltransferase]] |
| | [[Category: Rossmann fold]] | | [[Category: Rossmann fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:03:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 12:17:41 2008'' |
Revision as of 09:17, 1 July 2008
Template:STRUCTURE 1iir
Crystal Structure of UDP-glucosyltransferase GtfB
Template:ABSTRACT PUBMED 11470430
About this Structure
1IIR is a Single protein structure of sequence from Amycolatopsis orientalis. Full crystallographic information is available from OCA.
Reference
Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics., Mulichak AM, Losey HC, Walsh CT, Garavito RM, Structure. 2001 Jul 3;9(7):547-57. PMID:11470430
Page seeded by OCA on Tue Jul 1 12:17:41 2008
