| http://purl.uniprot.org/citations/15381072 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15381072 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15381072 | http://www.w3.org/2000/01/rdf-schema#comment | "The bacteriophage T4 alpha- and beta-glucosyltransferases (AGT and BGT) catalyse the transfer of glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine of T4 DNA in an alpha- and beta-conformation, respectively. Following the 3D structure of BGT and a secondary structure alignment of AGT and BGT, we performed a site-directed mutagenesis of AGT. A two-domain structure was deduced, with an open substrate-free and a closed substrate-bound conformation. We also identified specific amino acids involved in DNA binding. The identification of a protein-protein interaction of AGT and gp45 which is a part of the T4 replication complex supports the idea that T4 DNA is alpha-glucosylated immediately after synthesis. BGT then glucosylates those hydroxymethyl cytosines not previously served by AGT."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2004.08.170"xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2004.08.170"xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/author | "Depping R."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/author | "Depping R."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/author | "Piotrowski M."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/author | "Piotrowski M."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/author | "Ruger W."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/author | "Ruger W."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/author | "Sommer N."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/author | "Sommer N."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/pages | "809-815"xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/pages | "809-815"xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/title | "Bacteriophage T4 alpha-glucosyltransferase: a novel interaction with gp45 and aspects of the catalytic mechanism."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/title | "Bacteriophage T4 alpha-glucosyltransferase: a novel interaction with gp45 and aspects of the catalytic mechanism."xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/volume | "323"xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://purl.uniprot.org/core/volume | "323"xsd:string |
| http://purl.uniprot.org/citations/15381072 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15381072 |
| http://purl.uniprot.org/citations/15381072 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15381072 |