1NYC

Staphostatins resemble lipocalins, not cystatins in fold.

1NYC の概要

• エントリーDOI: 10.2210/pdb1nyc/pdb
• 分子名称: cysteine protease inhibitor, CHLORIDE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: staphostatin b, sspc, cysteine protease inhibitor, hydrolase inhibitor
• 由来する生物種: Staphylococcus aureus subsp. aureus
• 細胞内の位置: Cytoplasm (By similarity): Q7A189
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26316.21

構造登録者

Rzychon, M.,Filipek, R.,Sabat, A.,Kosowska, K.,Dubin, A.,Potempa, J.,Bochtler, M. (登録日: 2003-02-12, 公開日: 2003-09-30, 最終更新日: 2024-02-14)

主引用文献

Rzychon, M.,Filipek, R.,Sabat, A.,Kosowska, K.,Dubin, A.,Potempa, J.,Bochtler, M.
Staphostatins resemble lipocalins, not cystatins in fold.
Protein Sci., 12:2252-2256, 2003

PubMed Abstract: Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Here, we present the 1.4 A crystal structure of staphostatin B and show that the fold can be described as a fully closed, highly sheared eight-stranded beta-barrel. Thus, staphostatin B is related to beta-barrel domains that are involved in the inhibition or regulation of proteases of various catalytic types and to the superfamily of lipocalins/cytosolic fatty acid binding proteins. Unexpectedly for a cysteine protease inhibitor, staphostatin B is not significantly similar to cystatins.

PubMed: 14500882
DOI: 10.1110/ps.03247703

実験手法

X-RAY DIFFRACTION (1.4 Å)