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New page: left|200px<br /><applet load="2bgu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bgu, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:2bgu.jpg|left|200px]]<br /><applet load="2bgu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2bgu, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF THE DNA MODIFYING ENZYME BETA-GLUCOSYLTRANSFERASE IN THE PRESENCE AND ABSENCE OF THE SUBSTRATE URIDINE DIPHOSPHOGLUCOSE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE DNA MODIFYING ENZYME BETA-GLUCOSYLTRANSFERASE IN THE PRESENCE AND ABSENCE OF THE SUBSTRATE URIDINE DIPHOSPHOGLUCOSE==
Bacteriophage T4 beta-glucosyltransferase (EC 2.4.1.27) catalyses the, transfer of glucose from uridine diphosphoglucose to hydroxymethyl groups, of modified cytosine bases in T4 duplex DNA forming beta-glycosidic, linkages. The enzyme forms part of a phage DNA protection system. We have, solved and refined the crystal structure of recombinant, beta-glucosyltransferase to 2.2 A resolution in the presence and absence, of the substrate, uridine diphosphoglucose. The structure comprises two, domains of similar topology, each reminiscent of a nucleotide binding, fold. The two domains are separated by a central cleft which generates a, concave surface along one side of the molecule. The substrate-bound, complex reveals only clear electron density for the uridine diphosphate, portion of the substrate. The UDPG is bound in a pocket at the bottom of, the cleft between the two domains and makes extensive hydrogen bonding, contacts with residues of the C-terminal domain only. The domains undergo, a rigid body conformational change causing the structure to adopt a more, closed conformation upon ligand binding. The movement of the domains is, facilitated by a hinge region between residues 166 and 172. Electrostatic, surface potential calculations reveal a large positive potential along the, concave surface of the structure, suggesting a possible site for duplex, DNA interaction.
<StructureSection load='2bgu' size='340' side='right'caption='[[2bgu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2bgu]] 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=2BGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BGU FirstGlance]. <br>
2BGU 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 UDP as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BGU OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bgu OCA], [https://pdbe.org/2bgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bgu RCSB], [https://www.ebi.ac.uk/pdbsum/2bgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bgu ProSAT]</span></td></tr>
Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose., Vrielink A, Ruger W, Driessen HP, Freemont PS, EMBO J. 1994 Aug 1;13(15):3413-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8062817 8062817]
</table>
[[Category: Bacteriophage t4]]
== Function ==
[[Category: DNA beta-glucosyltransferase]]
[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.
[[Category: Single protein]]
__TOC__
[[Category: Driessen, H.P.C.]]
</StructureSection>
[[Category: Freemont, P.S.]]
[[Category: Escherichia virus T4]]
[[Category: Rueger, W.]]
[[Category: Large Structures]]
[[Category: Vrielink, A.]]
[[Category: Driessen HPC]]
[[Category: UDP]]
[[Category: Freemont PS]]
[[Category: transferase (glycosyltransferase)]]
[[Category: Rueger W]]
 
[[Category: Vrielink A]]
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