3EAY

Crystal structure of the human SENP7 catalytic domain

3EAY の概要

• エントリーDOI: 10.2210/pdb3eay/pdb
• 分子名称: Sentrin-specific protease 7, SULFATE ION (3 entities in total)
• 機能のキーワード: protease, sentrin-specific protease, ulp, senp, sumo, ubiquitin, crystal, alternative splicing, hydrolase, phosphoprotein, polymorphism, thiol protease, ubl conjugation pathway
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37933.91

構造登録者

Lima, C.D.,Reverter, D. (登録日: 2008-08-26, 公開日: 2008-09-16, 最終更新日: 2024-02-21)

主引用文献

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

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: 18799455
DOI: 10.1074/jbc.M805655200

実験手法

X-RAY DIFFRACTION (2.4 Å)