2ckh
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(New page: 200px<br /> <applet load="2ckh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ckh, resolution 3.20Å" /> '''SENP1-SUMO2 COMPLEX...)
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Revision as of 19:09, 12 November 2007
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SENP1-SUMO2 COMPLEX
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
2CKH is a Protein complex structure of sequences from Homo sapiens. This structure superseeds the now removed PDB entry 2BZO. 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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