4QPB

Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate

4QPB の概要

• エントリーDOI: 10.2210/pdb4qpb/pdb
• 関連するPDBエントリー: 1QWY 1R77 2B0P 2B13 2B44 3IT5 3IT7 4BH5 4LXC 4QP5
• 分子名称: Lysostaphin, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: peptidase family m23, peptidoglycan amidase, metallopeptidase, peptidoglycan, hydrolase, extracellular
• 由来する生物種: Staphylococcus simulans
• 細胞内の位置: Secreted: P10547
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30869.24

構造登録者

Sabala, I.,Jagielska, E.,Bardelang, P.T.,Czapinska, H.,Dahms, S.O.,Sharpe, J.A.,James, R.,Than, M.E.,Thomas, N.R.,Bochtler, M. (登録日: 2014-06-22, 公開日: 2014-07-09, 最終更新日: 2023-09-20)

主引用文献

Sabala, I.,Jagielska, E.,Bardelang, P.T.,Czapinska, H.,Dahms, S.O.,Sharpe, J.A.,James, R.,Than, M.E.,Thomas, N.R.,Bochtler, M.
Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans.
Febs J., 281:4112-4122, 2014

PubMed Abstract: Staphylococcus simulans biovar staphylolyticus lysostaphin efficiently cleaves Staphylococcus aureus cell walls. The protein is in late clinical trials as a topical anti-staphylococcal agent, and can be used to prevent staphylococcal growth on artificial surfaces. Moreover, the gene has been both stably engineered into and virally delivered to mice or livestock to obtain resistance against staphylococci. Here, we report the first crystal structure of mature lysostaphin and two structures of its isolated catalytic domain at 3.5, 1.78 and 1.26 Å resolution, respectively. The structure of the mature active enzyme confirms its expected organization into catalytic and cell-wall-targeting domains. It also indicates that the domains are mobile with respect to each other because of the presence of a highly flexible peptide linker. The high-resolution structures of the catalytic domain provide details of Zn(2+) coordination and may serve as a starting point for the engineering of lysostaphin variants with improved biotechnological characteristics.

PubMed: 25039253
DOI: 10.1111/febs.12929

実験手法

X-RAY DIFFRACTION (1.78 Å)