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| [[Image:1nvk.jpg|left|200px]]
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| {{Structure
| | ==T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution== |
| |PDB= 1nvk |SIZE=350|CAPTION= <scene name='initialview01'>1nvk</scene>, resolution 1.8Å
| | <StructureSection load='1nvk' size='340' side='right'caption='[[1nvk]], [[Resolution|resolution]] 1.80Å' scene=''> |
| |SITE= | | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
| | <table><tr><td colspan='2'>[[1nvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NVK FirstGlance]. <br> |
| |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]
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| |GENE= BGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4])
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> |
| }}
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nvk OCA], [https://pdbe.org/1nvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nvk RCSB], [https://www.ebi.ac.uk/pdbsum/1nvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nvk ProSAT]</span></td></tr> |
| | | </table> |
| '''T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution'''
| | == Function == |
| | | [https://www.uniprot.org/uniprot/GSTB_BPT4 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. |
| | | __TOC__ |
| ==Overview==
| | </StructureSection> |
| 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.
| | [[Category: Escherichia virus T4]] |
| | | [[Category: Large Structures]] |
| ==About this Structure==
| | [[Category: Gueguen-Chaignon V]] |
| 1NVK 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=1NVK OCA].
| | [[Category: Kurzeck J]] |
| | | [[Category: Lariviere L]] |
| ==Reference== | | [[Category: Morera S]] |
| 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: Rueger W]] |
| [[Category: Bacteriophage t4]] | |
| [[Category: DNA beta-glucosyltransferase]] | |
| [[Category: Single protein]]
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| [[Category: Gueguen-Chaignon, V.]] | |
| [[Category: Kurzeck, J.]] | |
| [[Category: Lariviere, L.]] | |
| [[Category: Morera, S.]] | |
| [[Category: Rueger, W.]] | |
| [[Category: GOL]]
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| [[Category: MN]]
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| [[Category: UDP]]
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| [[Category: glycosyltransferase]]
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| [[Category: gt-b]]
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| [[Category: mn]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:57:47 2008''
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