1X9Y

The prostaphopain B structure

1X9Y の概要

• エントリーDOI: 10.2210/pdb1x9y/pdb
• 関連するPDBエントリー: 1CV8 1PXV
• 分子名称: cysteine proteinase (2 entities in total)
• 機能のキーワード: half-barrel, barrel-sandwich-hybrid, hydrolase
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Secreted (By similarity): Q70UQ8
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 167386.02

構造登録者

Filipek, R.,Szczepanowski, R.,Sabat, A.,Potempa, J.,Bochtler, M. (登録日: 2004-08-24, 公開日: 2004-11-23, 最終更新日: 2023-08-23)

主引用文献

Filipek, R.,Szczepanowski, R.,Sabat, A.,Potempa, J.,Bochtler, M.
Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition.
Biochemistry, 43:14306-14315, 2004

PubMed Abstract: Prostaphopain B is the precursor of staphopain B, a papain-type secreted cysteine protease from the pathogen Staphylococcus aureus. Here, we describe the 2.5 A crystal structure of the proenzyme. Its 21 kDa proregion is organized around a central half-barrel or barrel-sandwich hybrid and occludes primed, but not nonprimed, sites in the active site cleft of the protease. The structure of the mature part of the protease is similar to previously reported staphopain structures, and no distortion of the catalytic residues is apparent at 2.5 A resolution. A comparison of prostaphopain B with the staphopain B-staphostatin B complex shows that the proregion and the inhibitor interact with largely nonoverlapping parts of the protease surface. In a modeled complex of prostaphopain B with staphostatin B, clashes occur both inside and outside the active site cleft, but involve mostly poorly ordered regions of the protein that may be mobile.

PubMed: 15518582
DOI: 10.1021/bi048661m

実験手法

X-RAY DIFFRACTION (2.5 Å)