1j39: Difference between revisions
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[[Image:1j39.jpg|left|200px]] | [[Image:1j39.jpg|left|200px]] | ||
'''Crystal Structure of T4 phage BGT in complex with its UDP-glucose substrate''' | {{Structure | ||
|PDB= 1j39 |SIZE=350|CAPTION= <scene name='initialview01'>1j39</scene>, resolution 1.87Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=UPG:URIDINE-5'-DIPHOSPHATE-GLUCOSE'>UPG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/DNA_beta-glucosyltransferase DNA beta-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.27 2.4.1.27] | |||
|GENE= BGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4]) | |||
}} | |||
'''Crystal Structure of T4 phage BGT in complex with its UDP-glucose substrate''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1J39 is a [ | 1J39 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J39 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism., Lariviere L, Gueguen-Chaignon V, Morera S, J Mol Biol. 2003 Jul 25;330(5):1077-86. PMID:[http:// | Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism., Lariviere L, Gueguen-Chaignon V, Morera S, J Mol Biol. 2003 Jul 25;330(5):1077-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12860129 12860129] | ||
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: DNA beta-glucosyltransferase]] | [[Category: DNA beta-glucosyltransferase]] | ||
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[[Category: udp-glucose]] | [[Category: udp-glucose]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:58:18 2008'' | ||
Revision as of 12:58, 20 March 2008
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| , resolution 1.87Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | BGT (Bacteriophage T4) | ||||||
| Activity: | DNA beta-glucosyltransferase, with EC number 2.4.1.27 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of T4 phage BGT in complex with its UDP-glucose substrate
OverviewOverview
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.
About this StructureAbout this Structure
1J39 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism., Lariviere L, Gueguen-Chaignon V, Morera S, J Mol Biol. 2003 Jul 25;330(5):1077-86. PMID:12860129
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