http://purl.uniprot.org/citations/15660128 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15660128 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15660128 | http://www.w3.org/2000/01/rdf-schema#comment | "E1 enzymes facilitate conjugation of ubiquitin and ubiquitin-like proteins through adenylation, thioester transfer within E1, and thioester transfer from E1 to E2 conjugating proteins. Structures of human heterodimeric Sae1/Sae2-Mg.ATP and Sae1/Sae2-SUMO-1-Mg.ATP complexes were determined at 2.2 and 2.75 A resolution, respectively. Despite the presence of Mg.ATP, the Sae1/Sae2-SUMO-1-Mg.ATP structure reveals a substrate complex insomuch as the SUMO C-terminus remains unmodified within the adenylation site and 35 A from the catalytic cysteine, suggesting that additional changes within the adenylation site may be required to facilitate chemistry prior to adenylation and thioester transfer. A mechanism for E2 recruitment to E1 is suggested by biochemical and genetic data, each of which supports a direct role for the E1 C-terminal ubiquitin-like domain for E2 recruitment during conjugation."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.emboj.7600552"xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.emboj.7600552"xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/author | "Lima C.D."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/author | "Lima C.D."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/author | "Lois L.M."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/author | "Lois L.M."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/pages | "439-451"xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/pages | "439-451"xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/title | "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/title | "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/volume | "24"xsd:string |
http://purl.uniprot.org/citations/15660128 | http://purl.uniprot.org/core/volume | "24"xsd:string |
http://purl.uniprot.org/citations/15660128 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15660128 |
http://purl.uniprot.org/citations/15660128 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15660128 |
http://purl.uniprot.org/citations/15660128 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15660128 |
http://purl.uniprot.org/citations/15660128 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15660128 |
http://purl.uniprot.org/uniprot/Q9UBE0 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15660128 |
http://purl.uniprot.org/uniprot/P63165 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15660128 |