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==T4 phage BGT-D100A mutant in complex with UDP-glucose: Form II== | ==T4 phage BGT-D100A mutant in complex with UDP-glucose: Form II== | ||
<StructureSection load='1nzf' size='340' side='right' caption='[[1nzf]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1nzf' size='340' side='right' caption='[[1nzf]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nzf OCA], [http://pdbe.org/1nzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nzf RCSB], [http://www.ebi.ac.uk/pdbsum/1nzf PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nzf OCA], [http://pdbe.org/1nzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nzf RCSB], [http://www.ebi.ac.uk/pdbsum/1nzf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nzf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1nzf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1nzf" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:02, 1 November 2017
T4 phage BGT-D100A mutant in complex with UDP-glucose: Form IIT4 phage BGT-D100A mutant in complex with UDP-glucose: Form II
Structural highlights
Function[GSTB_BPT4] Catalyzes the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA. Is involved in a DNA modification process to protect the phage genome against its own nucleases and the host restriction endonuclease system. Publication Abstract from PubMedT4 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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