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http://purl.uniprot.org/citations/8062817http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8062817http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8062817http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1994.tb06646.x"xsd:string
http://purl.uniprot.org/citations/8062817http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1994.tb06646.x"xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/author"Rueger W."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/author"Rueger W."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/author"Driessen H.P.C."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/author"Driessen H.P.C."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/author"Freemont P.S."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/author"Freemont P.S."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/author"Vrelink A."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/author"Vrelink A."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/pages"3413-3422"xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/pages"3413-3422"xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/title"Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/title"Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose."xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/8062817http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/8062817http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8062817
http://purl.uniprot.org/citations/8062817http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8062817