| http://purl.uniprot.org/citations/16712526 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16712526 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16712526 | http://www.w3.org/2000/01/rdf-schema#comment | "SUMO (small ubiquitin-related modifier)-specific proteases catalyse the maturation and de-conjugation processes of the sumoylation pathway and modulate various cellular responses including nuclear metabolism and cell cycle progression. The active-site cysteine residue is conserved among all known SUMO-specific proteases and is not substitutable by serine in the hydrolysis reactions demonstrated previously in yeast. We report here that the catalytic domain of human protease SENP1 (SUMO-specific protease 1) mutant SENP1C(C603S) carrying a mutation of cysteine to serine at the active site is inactive in maturation and de-conjugation reactions. To further understand the hydrolytic mechanism catalysed by SENP1, we have determined, at 2.8 A resolution (1 A = 0.1 nm), the X-ray structure of SENP1C(C603S)-SUMO-1 complex. A comparison of the structure of SENP2-SUMO-1 suggests strongly that SUMO-specific proteases require a self-conformational change prior to cleavage of peptide or isopeptide bond in the maturation and de-conjugation processes respectively. Moreover, analysis of the interface of SENP1 and SUMO-1 has led to the identification of four unique amino acids in SENP1 that facilitate the binding of SUMO-1. By means of an in vitro assay, we further demonstrate a novel function of SENP1 in hydrolysing the thioester linkage in E1-SUMO and E2-SUMO complexes. The results disclose a new mechanism of regulation of the sumoylation pathway by the SUMO-specific proteases."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20060526"xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20060526"xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Chan H.Y."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Chan H.Y."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Ng T.B."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Ng T.B."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Xu Z."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Xu Z."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Lam K.H."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Lam K.H."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Au S.W.N."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Au S.W.N."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Chau S.F."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/author | "Chau S.F."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/pages | "345-352"xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/pages | "345-352"xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/title | "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease."xsd:string |
| http://purl.uniprot.org/citations/16712526 | http://purl.uniprot.org/core/title | "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease."xsd:string |