2IO2

Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1

2IO2 の概要

• エントリーDOI: 10.2210/pdb2io2/pdb
• 関連するPDBエントリー: 1TGZ 2IO0 2IO1 2IO3
• 分子名称: Sentrin-specific protease 2, Small ubiquitin-related modifier 1, Ran GTPase-activating protein 1, ... (4 entities in total)
• 機能のキーワード: sumo, ubiquitin, senp, ulp, complex, protein binding, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus, nuclear pore complex : Q9HC62; Nucleus membrane: P63165; Cytoplasm: P46060
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 55486.97

構造登録者

Reverter, D.,Lima, C.D. (登録日: 2006-10-09, 公開日: 2006-11-21, 最終更新日: 2023-08-30)

主引用文献

Reverter, D.,Lima, C.D.
Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates.
Nat.Struct.Mol.Biol., 13:1060-1068, 2006

PubMed 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.

PubMed: 17099700
DOI: 10.1038/nsmb1168

実験手法

X-RAY DIFFRACTION (2.9 Å)