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1nzf
From Proteopedia
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| - | [[Image:1nzf.gif|left|200px]] | + | [[Image:1nzf.gif|left|200px]] |
| - | + | ||
| - | '''T4 phage BGT-D100A mutant in complex with UDP-glucose: Form II''' | + | {{Structure |
| + | |PDB= 1nzf |SIZE=350|CAPTION= <scene name='initialview01'>1nzf</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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]) | ||
| + | }} | ||
| + | |||
| + | '''T4 phage BGT-D100A mutant in complex with UDP-glucose: Form II''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NZF is a [ | + | 1NZF 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=1NZF 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 13:03:43 2008'' |
Revision as of 11:03, 20 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | BGT (Bacteriophage T4) | ||||||
| Activity: | DNA beta-glucosyltransferase, with EC number 2.4.1.27 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
T4 phage BGT-D100A mutant in complex with UDP-glucose: Form II
Overview
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 Structure
1NZF is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
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:12860129
Page seeded by OCA on Thu Mar 20 13:03:43 2008
