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| - | [[Image:2bgu.jpg|left|200px]] | |
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| - | {{Structure
| + | ==CRYSTAL STRUCTURE OF THE DNA MODIFYING ENZYME BETA-GLUCOSYLTRANSFERASE IN THE PRESENCE AND ABSENCE OF THE SUBSTRATE URIDINE DIPHOSPHOGLUCOSE== |
| - | |PDB= 2bgu |SIZE=350|CAPTION= <scene name='initialview01'>2bgu</scene>, resolution 2.2Å
| + | <StructureSection load='2bgu' size='340' side='right'caption='[[2bgu]], [[Resolution|resolution]] 2.20Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene>
| + | <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> |
| - | |ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | |GENE= | + | <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> |
| - | |DOMAIN=
| + | <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> |
| - | |RELATEDENTRY= | + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bgu OCA], [http://www.ebi.ac.uk/pdbsum/2bgu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bgu RCSB]</span>
| + | == 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__ |
| - | '''CRYSTAL STRUCTURE OF THE DNA MODIFYING ENZYME BETA-GLUCOSYLTRANSFERASE IN THE PRESENCE AND ABSENCE OF THE SUBSTRATE URIDINE DIPHOSPHOGLUCOSE'''
| + | </StructureSection> |
| - | | + | [[Category: Escherichia virus T4]] |
| - | | + | [[Category: Large Structures]] |
| - | ==Overview==
| + | [[Category: Driessen HPC]] |
| - | 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.
| + | [[Category: Freemont PS]] |
| - | | + | [[Category: Rueger W]] |
| - | ==About this Structure==
| + | [[Category: Vrielink A]] |
| - | 2BGU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BGU OCA].
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| - | | + | |
| - | ==Reference== | + | |
| - | 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://www.ncbi.nlm.nih.gov/pubmed/8062817 8062817]
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| - | [[Category: DNA beta-glucosyltransferase]]
| + | |
| - | [[Category: Enterobacteria phage t4]] | + | |
| - | [[Category: Single protein]] | + | |
| - | [[Category: Driessen, H P.C.]] | + | |
| - | [[Category: Freemont, P S.]] | + | |
| - | [[Category: Rueger, W.]] | + | |
| - | [[Category: Vrielink, A.]] | + | |
| - | [[Category: transferase (glycosyltransferase)]]
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| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:06:13 2008''
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