1PXV

The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease

1PXV の概要

• エントリーDOI: 10.2210/pdb1pxv/pdb
• 関連するPDBエントリー: 1CV8 1NYC
• 分子名称: cysteine protease, cysteine protease Inhibitor, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: cysteine protease inhibitor, hydrolase
• 由来する生物種: Staphylococcus aureus; 詳細
• 細胞内の位置: Secreted (By similarity): Q70UQ8; Cytoplasm: Q9EYW6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68812.79

構造登録者

Filipek, R.,Rzychon, M.,Oleksy, A.,Gruca, M.,Dubin, A.,Potempa, J.,Bochtler, M. (登録日: 2003-07-07, 公開日: 2003-10-21, 最終更新日: 2023-08-16)

主引用文献

Filipek, R.,Rzychon, M.,Oleksy, A.,Gruca, M.,Dubin, A.,Potempa, J.,Bochtler, M.
The Staphostatin-Staphopain Complex: A FORWARD BINDING INHIBITOR IN COMPLEX WITH ITS TARGET CYSTEINE PROTEASE.
J.Biol.Chem., 278:40959-40966, 2003

PubMed Abstract: Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Our recent crystal structure of staphostatin B has shown that this inhibitor forms a mixed, eight-stranded beta-barrel with statistically significant similarity to lipocalins, but not to cystatins. We now present the 1.8-A crystal structure of staphostatin B in complex with an inactive mutant of its target protease. The complex is held together through extensive interactions and buries a total surface area of 2300 A2. Unexpectedly for a cysteine protease inhibitor, staphostatin B binds to staphopain B in an almost substrate-like manner. The inhibitor polypeptide chain runs through the protease active site cleft in the forward direction, with residues IG-TS in P2 to P2' positions. Both in the free and complexed forms, the P1 glycine residue of the inhibitor is in a main chain conformation only accessible to glycines. Mutations in this residue lead to a loss of affinity of the inhibitor for protease and convert the inhibitor into a substrate.

PubMed: 12874290
DOI: 10.1074/jbc.M302926200

実験手法

X-RAY DIFFRACTION (1.8 Å)