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2g4d

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[[Image:2g4d.gif|left|200px]]<br /><applet load="2g4d" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2g4d.gif|left|200px]]
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caption="2g4d, resolution 2.800&Aring;" />
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'''Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1'''<br />
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{{Structure
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|PDB= 2g4d |SIZE=350|CAPTION= <scene name='initialview01'>2g4d</scene>, resolution 2.800&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2G4D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4D OCA].
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2G4D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4D OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16712526 16712526]
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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]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: ubiquitin-like protein]]
[[Category: ubiquitin-like protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:00:15 2008''

Revision as of 15:00, 20 March 2008


PDB ID 2g4d

Drag the structure with the mouse to rotate
, resolution 2.800Å
Coordinates: save as pdb, mmCIF, xml



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


Contents

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.

Disease

Known diseases associated with this structure: Orofacial cleft 10 OMIM:[601912]

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

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