3EAY
Crystal structure of the human SENP7 catalytic domain
Summary for 3EAY
| Entry DOI | 10.2210/pdb3eay/pdb |
| Descriptor | Sentrin-specific protease 7, SULFATE ION (3 entities in total) |
| Functional Keywords | protease, sentrin-specific protease, ulp, senp, sumo, ubiquitin, crystal, alternative splicing, hydrolase, phosphoprotein, polymorphism, thiol protease, ubl conjugation pathway |
| Biological source | Homo sapiens |
| Total number of polymer chains | 1 |
| Total formula weight | 37933.91 |
| Authors | Lima, C.D.,Reverter, D. (deposition date: 2008-08-26, release date: 2008-09-16, Last modification date: 2024-02-21) |
| Primary citation | Lima, C.D.,Reverter, D. Structure of the Human SENP7 Catalytic Domain and Poly-SUMO Deconjugation Activities for SENP6 and SENP7. J.Biol.Chem., 283:32045-32055, 2008 Cited by PubMed Abstract: Small ubiquitin-like modifier (SUMO) proteases regulate the abundance and lifetime of SUMO-conjugated substrates by antagonizing reactions catalyzed by SUMO-conjugating enzymes. Six SUMO proteases constitute the human SENP/ULP protease family (SENP1-3 and SENP5-7). SENP6 and SENP7 include the most divergent class of SUMO proteases, which also includes the yeast enzyme ULP2. We present the crystal structure of the SENP7 catalytic domain at a resolution of 2.4 angstroms. Comparison with structures of human SENP1 and SENP2 reveals unique elements that differ from previously characterized structures of SUMO-deconjugating enzymes. Biochemical assays show that SENP6 and SENP7 prefer SUMO2 or SUMO3 in deconjugation reactions with rates comparable with those catalyzed by SENP2, particularly during cleavage of di-SUMO2, di-SUMO3, and poly-SUMO chains composed of SUMO2 or SUMO3. In contrast, SENP6 and SENP7 exhibit lower rates for processing pre-SUMO1, pre-SUMO2, or pre-SUMO3 in comparison with SENP2. Structure-guided mutational analysis reveals elements unique to the SENP6 and SENP7 subclass of SENP/ULP proteases that contribute to protease function during deconjugation of poly-SUMO chains. PubMed: 18799455DOI: 10.1074/jbc.M805655200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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