2g4d: Difference between revisions
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{{STRUCTURE_2g4d| PDB=2g4d | SCENE= }} | |||
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'''Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1''' | '''Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1''' | ||
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[[Category: Lam, K H.]] | [[Category: Lam, K H.]] | ||
[[Category: Xu, Z.]] | [[Category: Xu, Z.]] | ||
[[Category: | [[Category: Protease]] | ||
[[Category: | [[Category: Sumo deconjugation]] | ||
[[Category: | [[Category: Sumo maturation]] | ||
[[Category: | [[Category: Ubiquitin-like protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:40:40 2008'' | |||
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Revision as of 01:40, 4 May 2008
Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1
Overview
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.
About this Structure
2G4D is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease., Xu Z, Chau SF, Lam KH, Chan HY, Ng TB, Au SW, Biochem J. 2006 Sep 15;398(3):345-52. PMID:16712526 Page seeded by OCA on Sun May 4 04:40:40 2008
