2ckg
From Proteopedia
(New page: 200px<br /> <applet load="2ckg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ckg, resolution 2.45Å" /> '''THE STRUCTURE OF SE...) |
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| - | [[Image:2ckg.gif|left|200px]]<br /> | + | [[Image:2ckg.gif|left|200px]]<br /><applet load="2ckg" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ckg" size=" | + | |
caption="2ckg, resolution 2.45Å" /> | caption="2ckg, resolution 2.45Å" /> | ||
'''THE STRUCTURE OF SENP1 SUMO-2 CO-COMPLEX SUGGESTS A STRUCTURAL BASIS FOR DISCRIMINATION BETWEEN SUMO PARALOGUES DURING PROCESSING'''<br /> | '''THE STRUCTURE OF SENP1 SUMO-2 CO-COMPLEX SUGGESTS A STRUCTURAL BASIS FOR DISCRIMINATION BETWEEN SUMO PARALOGUES DURING PROCESSING'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The SUMO (small ubiquitin-like modifier)-specific protease SENP1 | + | The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity. |
==About this Structure== | ==About this Structure== | ||
| - | 2CKG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure | + | 2CKG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 2BZP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dong, C.]] | [[Category: Dong, C.]] | ||
| - | [[Category: Naismith, J | + | [[Category: Naismith, J H.]] |
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: nuclear protein]] | [[Category: nuclear protein]] | ||
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[[Category: ubl conjugation pathway]] | [[Category: ubl conjugation pathway]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:32 2008'' |
Revision as of 14:49, 21 February 2008
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THE STRUCTURE OF SENP1 SUMO-2 CO-COMPLEX SUGGESTS A STRUCTURAL BASIS FOR DISCRIMINATION BETWEEN SUMO PARALOGUES DURING PROCESSING
Overview
The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity.
About this Structure
2CKG is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2BZP. Full crystallographic information is available from OCA.
Reference
The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing., Shen LN, Dong C, Liu H, Naismith JH, Hay RT, Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580
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