1tgz
From Proteopedia
(New page: 200px<br /> <applet load="1tgz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tgz, resolution 2.80Å" /> '''Structure of human ...) |
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caption="1tgz, resolution 2.80Å" /> | caption="1tgz, resolution 2.80Å" /> | ||
'''Structure of human Senp2 in complex with SUMO-1'''<br /> | '''Structure of human Senp2 in complex with SUMO-1'''<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== | ||
| - | 1TGZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TGZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Lima, C | + | [[Category: Lima, C D.]] |
[[Category: Reverter, D.]] | [[Category: Reverter, D.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[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 15:13:23 2008'' |
Revision as of 13:13, 21 February 2008
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Structure of human Senp2 in complex with SUMO-1
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
1TGZ is a Protein complex structure of sequences from Homo sapiens with as ligand. 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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