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| [[Image:1nvk.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1nvk| PDB=1nvk | SCENE= }} | | {{STRUCTURE_1nvk| PDB=1nvk | SCENE= }} |
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| '''T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution'''
| | ===T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution=== |
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| ==Overview==
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| T4 phage beta-glucosyltransferase (BGT) is an inverting glycosyltransferase (GT) that transfers glucose from uridine diphospho-glucose (UDP-glucose) to an acceptor modified DNA. BGT belongs to the GT-B structural superfamily, represented, so far, by five different inverting or retaining GT families. Here, we report three high-resolution X-ray structures of BGT and a point mutant solved in the presence of UDP-glucose. The two co-crystal structures of the D100A mutant show that, unlike the wild-type enzyme, this mutation prevents glucose hydrolysis. This strongly indicates that Asp100 is the catalytic base. We obtained the wild-type BGT-UDP-glucose complex by soaking substrate-free BGT crystals. Comparison with a previous structure of BGT solved in the presence of the donor product UDP and an acceptor analogue provides the first model of an inverting GT-B enzyme in which both the donor and acceptor substrates are bound to the active site. The structural analyses support the in-line displacement reaction mechanism previously proposed, locate residues involved in donor substrate specificity and identify the catalytic base.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12860129}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12860129 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12860129}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Gt-b]] | | [[Category: Gt-b]] |
| [[Category: Mn]] | | [[Category: Mn]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:01:52 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:32:07 2008'' |
