1tgz
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(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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Revision as of 17:18, 12 November 2007
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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 SO4 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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