2io0
Crystal structure of human Senp2 in complex with preSUMO-2
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OverviewOverview
SUMO processing and deconjugation are essential proteolytic activities for, nuclear metabolism and cell-cycle progression in yeast and higher, eukaryotes. To elucidate the mechanisms used during substrate lysine, deconjugation, SUMO isoform processing and SUMO isoform interactions, X-ray structures were determined for a catalytically inert SENP2 protease, domain in complex with conjugated RanGAP1-SUMO-1 or RanGAP1-SUMO-2, or in, complex with SUMO-2 or SUMO-3 precursors. Common features within the, active site include a 90 degrees kink proximal to the scissile bond that, forces C-terminal amino acid residues or the lysine side chain toward a, protease surface that appears optimized for lysine deconjugation. Analysis, of this surface reveals SENP2 residues, particularly Met497, that mediate, and in some instances reverse, in vitro substrate specificity. Mutational, analysis and biochemistry provide a mechanism for SENP2 substrate, preferences that explains why SENP2 catalyzes SUMO deconjugation more, efficiently than processing.
About this StructureAbout this Structure
2IO0 is a Protein complex structure of sequences from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates., Reverter D, Lima CD, Nat Struct Mol Biol. 2006 Dec;13(12):1060-8. Epub 2006 Nov 12. PMID:17099700
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