2IO1: Crystal Structure Of Human Senp2 In Complex With Presumo-3

Citation:
Abstract
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.
PDB ID: 2IO1Download
MMDB ID: 42980
PDB Deposition Date: 2006/10/9
Updated in MMDB: 2006/12
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Similar Structures:
Biological Unit for 2IO1: dimeric; determined by author and by software (PISA)
Molecular Components in 2IO1
Label Count Molecule
Proteins (2 molecules)
1
Sentrin-specific Protease 2(Gene symbol: SENP2)
Molecule annotation
1
Small Ubiquitin-related Modifier 3 Precursor(Gene symbol: SUMO3)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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