2hkp

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{{STRUCTURE_2hkp| PDB=2hkp | SCENE= }}
{{STRUCTURE_2hkp| PDB=2hkp | SCENE= }}
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'''SUMO protease Ulp1 with the catalytic cysteine oxidized to a sulfenic acid'''
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===SUMO protease Ulp1 with the catalytic cysteine oxidized to a sulfenic acid===
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==Overview==
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Sumoylation has emerged as an indispensable post-translational modification that modulates the functions of a broad spectrum of proteins. Recent studies have demonstrated that reactive oxygen species influence the equilibrium of sumoylation-desumoylation. We show herein that H2O2 induces formation of an intermolecular disulfide linkage of human SUMO protease SENP1 via the active-site Cys 603 and a unique residue Cys 613. Such reversible modification confers a higher recovery of enzyme activity, which is also observed in yeast Ulp1, but not in human SENP2, suggesting its protective role against irreversible sulfhydryl oxidation. In vivo formation of a disulfide-linked dimer of SENP1 is also detected in cultured cells in response to oxidative stress. The modifications are further elucidated by the crystal structures of Ulp1 with the catalytic cysteine oxidized to sulfenic, sulfinic, and sulfonic acids. Our findings suggest that, in addition to SUMO conjugating enzymes, SUMO proteases may act as redox sensors and effectors modulating the desumoylation pathway and specific cellular responses to oxidative stress.
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{{ABSTRACT_PUBMED_17704192}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation., Xu Z, Lam LS, Lam LH, Chau SF, Ng TB, Au SW, FASEB J. 2008 Jan;22(1):127-37. Epub 2007 Aug 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17704192 17704192]
Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation., Xu Z, Lam LS, Lam LH, Chau SF, Ng TB, Au SW, FASEB J. 2008 Jan;22(1):127-37. Epub 2007 Aug 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17704192 17704192]
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Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast., Mossessova E, Lima CD, Mol Cell. 2000 May;5(5):865-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10882122 10882122]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Xu, Z.]]
[[Category: Xu, Z.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:02:08 2008''

Revision as of 06:02, 28 July 2008

Image:2hkp.png

Template:STRUCTURE 2hkp

SUMO protease Ulp1 with the catalytic cysteine oxidized to a sulfenic acid

Template:ABSTRACT PUBMED 17704192

About this Structure

2HKP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation., Xu Z, Lam LS, Lam LH, Chau SF, Ng TB, Au SW, FASEB J. 2008 Jan;22(1):127-37. Epub 2007 Aug 17. PMID:17704192

Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast., Mossessova E, Lima CD, Mol Cell. 2000 May;5(5):865-76. PMID:10882122

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