2g4d

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{{STRUCTURE_2g4d| PDB=2g4d | SCENE= }}
{{STRUCTURE_2g4d| PDB=2g4d | SCENE= }}
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'''Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1'''
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===Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16712526}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16712526 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16712526}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16712526 16712526]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16712526 16712526]
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Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1., Xu Z, Au SW, Biochem J. 2005 Mar 1;386(Pt 2):325-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15487983 15487983]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Sumo maturation]]
[[Category: Sumo maturation]]
[[Category: Ubiquitin-like protein]]
[[Category: Ubiquitin-like protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:40:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:56:12 2008''

Revision as of 20:56, 28 July 2008

Image:2g4d.png

Template:STRUCTURE 2g4d

Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1

Template:ABSTRACT PUBMED 16712526

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

Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1., Xu Z, Au SW, Biochem J. 2005 Mar 1;386(Pt 2):325-30. PMID:15487983

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