| http://purl.uniprot.org/citations/16081100 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16081100 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16081100 | http://www.w3.org/2000/01/rdf-schema#comment | "The Escherichia coli T4 bacteriophage uses two glycosyltransferases to glucosylate and thus protect its DNA: the retaining alpha-glucosyltransferase (AGT) and the inverting beta-glucosyltransferase (BGT). They glucosylate 5-hydroxymethyl cytosine (5-HMC) bases of duplex DNA using UDP-glucose as the sugar donor to form an alpha-glucosidic linkage and a beta-glucosidic linkage, respectively. Five structures of AGT have been determined: a binary complex with the UDP product and four ternary complexes with UDP or UDP-glucose and oligonucleotides containing an A:G, HMU:G (hydroxymethyl uracyl) or AP:G (apurinic/apyrimidinic) mismatch at the target base-pair. AGT adopts the GT-B fold, one of the two folds known for GTs. However, while the sugar donor binding mode is classical for a GT-B enzyme, the sugar acceptor binding mode is unexpected and breaks the established consensus: AGT is the first GT-B enzyme that predominantly binds both the sugar donor and acceptor to the C-terminal domain. Its active site pocket is highly similar to four retaining GT-B glycosyltransferases (trehalose-6-phosphate synthase, glycogen synthase, glycogen and maltodextrin phosphorylases) strongly suggesting a common evolutionary origin and catalytic mechanism for these enzymes. Structure-guided mutagenesis and kinetic analysis do not permit identification of a nucleophile residue responsible for a glycosyl-enzyme intermediate for the classical double displacement mechanism. Interestingly, the DNA structures reveal partially flipped-out bases. They provide evidence for a passive role of AGT in the base-flipping mechanism and for its specific recognition of the acceptor base."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2005.07.007"xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2005.07.007"xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/author | "Morera S."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/author | "Morera S."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/author | "Sommer N."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/author | "Sommer N."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/author | "Lariviere L."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/author | "Lariviere L."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/pages | "139-150"xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/pages | "139-150"xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/title | "Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/title | "Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase."xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/volume | "352"xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://purl.uniprot.org/core/volume | "352"xsd:string |
| http://purl.uniprot.org/citations/16081100 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16081100 |
| http://purl.uniprot.org/citations/16081100 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16081100 |
| http://purl.uniprot.org/citations/16081100 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16081100 |
| http://purl.uniprot.org/citations/16081100 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16081100 |