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1j39

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[[Image:1j39.jpg|left|200px]]<br /><applet load="1j39" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j39.jpg|left|200px]]
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caption="1j39, resolution 1.87&Aring;" />
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'''Crystal Structure of T4 phage BGT in complex with its UDP-glucose substrate'''<br />
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{{Structure
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|PDB= 1j39 |SIZE=350|CAPTION= <scene name='initialview01'>1j39</scene>, resolution 1.87&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=UPG:URIDINE-5'-DIPHOSPHATE-GLUCOSE'>UPG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE= BGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4])
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}}
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'''Crystal Structure of T4 phage BGT in complex with its UDP-glucose substrate'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1J39 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=UPG:'>UPG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J39 OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12860129 12860129]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:58:18 2008''

Revision as of 09:58, 20 March 2008


PDB ID 1j39

Drag the structure with the mouse to rotate
, 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


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

1J39 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

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