| http://purl.uniprot.org/citations/15023335 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15023335 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15023335 | http://www.w3.org/2000/01/rdf-schema#comment | "Sir2 proteins form a family of NAD(+)-dependent protein deacetylases required for diverse biological processes, including transcriptional silencing, suppression of rDNA recombination, control of p53 activity, regulation of acetyl-CoA synthetase, and aging. Although structures of Sir2 enzymes in the presence and absence of peptide substrate or NAD(+) have been determined, the role of the enzyme in the mechanism of deacetylation and NAD(+) cleavage is still unclear. Here, we present additional structures of Sir2Af2 in several differently complexed states: in a productive complex with NAD(+), in a nonproductive NAD(+) complex with bound ADP-ribose, and in the unliganded state. We observe a new mode of NAD(+) binding that seems to depend on acetyl-lysine binding, in which the nicotinamide ring of NAD(+) is buried in the highly conserved "C" pocket of the enzyme. We propose a detailed structure-based mechanism for deacetylation and nicotinamide inhibition of Sir2 consistent with mutagenesis and enzymatic studies."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1097-2765(04)00082-6"xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1097-2765(04)00082-6"xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/author | "Avalos J.L."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/author | "Avalos J.L."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/author | "Wolberger C."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/author | "Wolberger C."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/author | "Boeke J.D."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/author | "Boeke J.D."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/pages | "639-648"xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/pages | "639-648"xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/title | "Structural basis for the mechanism and regulation of Sir2 enzymes."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/title | "Structural basis for the mechanism and regulation of Sir2 enzymes."xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/15023335 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15023335 |
| http://purl.uniprot.org/citations/15023335 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15023335 |
| http://purl.uniprot.org/citations/15023335 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15023335 |
| http://purl.uniprot.org/citations/15023335 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15023335 |