1th0
From Proteopedia
(New page: 200px<br /> <applet load="1th0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1th0, resolution 2.20Å" /> '''Structure of human ...) |
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| - | [[Image:1th0.gif|left|200px]]<br /> | + | [[Image:1th0.gif|left|200px]]<br /><applet load="1th0" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1th0" size=" | + | |
caption="1th0, resolution 2.20Å" /> | caption="1th0, resolution 2.20Å" /> | ||
'''Structure of human Senp2'''<br /> | '''Structure of human Senp2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Modification of cellular proteins by the ubiquitin-like protein SUMO is | + | Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear metabolism and cell cycle progression in yeast. X-ray structures of the human Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 revealed details of the respective protease and substrate surfaces utilized in interactions between these two proteins. Comparative biochemical and structural analysis between Senp2 and the yeast SUMO protease Ulp1 revealed differential abilities to process SUMO-1, SUMO-2, and SUMO-3 in maturation and deconjugation reactions. Further biochemical characterization of the three SUMO isoforms into which an additional Gly-Gly di-peptide was inserted, or whereby the respective SUMO tails from the three isoforms were swapped, suggests a strict dependence for SUMO isopeptidase activity on residues C-terminal to the conserved Gly-Gly motif and preferred cleavage site for SUMO proteases. |
==About this Structure== | ==About this Structure== | ||
| - | 1TH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1TH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1TH0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lima, C | + | [[Category: Lima, C D.]] |
[[Category: Reverter, D.]] | [[Category: Reverter, D.]] | ||
[[Category: sumo; axam; senp; ulp; protease]] | [[Category: sumo; axam; senp; ulp; protease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:30 2008'' |
Revision as of 13:13, 21 February 2008
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Structure of human Senp2
Overview
Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear metabolism and cell cycle progression in yeast. X-ray structures of the human Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 revealed details of the respective protease and substrate surfaces utilized in interactions between these two proteins. Comparative biochemical and structural analysis between Senp2 and the yeast SUMO protease Ulp1 revealed differential abilities to process SUMO-1, SUMO-2, and SUMO-3 in maturation and deconjugation reactions. Further biochemical characterization of the three SUMO isoforms into which an additional Gly-Gly di-peptide was inserted, or whereby the respective SUMO tails from the three isoforms were swapped, suggests a strict dependence for SUMO isopeptidase activity on residues C-terminal to the conserved Gly-Gly motif and preferred cleavage site for SUMO proteases.
About this Structure
1TH0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex., Reverter D, Lima CD, Structure. 2004 Aug;12(8):1519-31. PMID:15296745
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