1M72

Crystal Structure of Caspase-1 from Spodoptera frugiperda

1M72 の概要

• エントリーDOI: 10.2210/pdb1m72/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000238
• 分子名称: Caspase-1, Ace-Asp-Glu-Val-Asp-chloromethylketone, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: caspase, cysteine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Spodoptera frugiperda (fall armyworm); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 94390.55

構造登録者

Forsyth, C.M.,Lemongello, D.,Friesen, P.D.,Fisher, A.J. (登録日: 2002-07-18, 公開日: 2004-01-20, 最終更新日: 2024-10-09)

主引用文献

Forsyth, C.M.,Lemongello, D.,LaCount, D.J.,Friesen, P.D.,Fisher, A.J.
Crystal structure of an invertebrate caspase.
J.Biol.Chem., 279:7001-7008, 2004

PubMed Abstract: Caspases play an essential role in the execution of apoptosis. These cysteine proteases are highly conserved among metazoans and are translated as inactive zymogens, which are activated by proteolytic cleavages to generate the large and small subunits and remove the N-terminal prodomain. The 2.3 A resolution crystal structure of active Sf-caspase-1, the principal effector caspase of the insect Spodoptera frugiperda, is presented here. The structure represents the first nonhuman caspase to be resolved. The structure of the cleaved and active protease was determined with the tetrapeptide inhibitor N-acetyl-Asp-Glu-Val-Asp-chloromethylketone covalently bonded to the active site cysteine. As expected, the overall fold of Sf-caspase-1 is exceedingly similar to that of the five active caspases from humans solved to date. The overall structure and active site arrangement of Sf-caspase-1 is most comparable with that of the human effector caspases, with which it shares highest sequence homology. The most prominent structural difference with Sf-caspase-1 is the position of the N-terminal region of the large subunit. Unlike the N terminus of human caspases, the N terminus of Sf-caspase-1 originates from the active site side where it interacts with active site loop L2 and then extends to the backside of the heterodimer. This unusual structural arrangement raises the possibility that the N-terminal prodomain plays a regulatory role during effector caspase activation or enzyme activity in insects.

PubMed: 14645217
DOI: 10.1074/jbc.M312472200

実験手法

X-RAY DIFFRACTION (2.3 Å)