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6RK4

Lysostaphin SH3b P4-G5 complex, synchrotron dataset

6RK4 の概要
エントリーDOI10.2210/pdb6rk4/pdb
分子名称Lysostaphin, (2~{R})-2-[[(2~{S})-2-[[(4~{R})-5-azanyl-4-[[(2~{S})-2-azanylpropanoyl]amino]-5-oxidanylidene-pentanoyl]amino]-6-[2-[2-[2-[2-(2-azanylethanoylamino)ethanoylamino]ethanoylamino]ethanoylamino]ethanoylamino]hexanoyl]amino]propanoic acid, 1,2-ETHANEDIOL, ... (4 entities in total)
機能のキーワードpeptidoglycan hydrolase, peptide binding protein
由来する生物種Staphylococcus simulans
タンパク質・核酸の鎖数1
化学式量合計53972.33
構造登録者
Walters-Morgan, H.,Lovering, A.L. (登録日: 2019-04-30, 公開日: 2019-10-16, 最終更新日: 2024-01-24)
主引用文献Gonzalez-Delgado, L.S.,Walters-Morgan, H.,Salamaga, B.,Robertson, A.J.,Hounslow, A.M.,Jagielska, E.,Sabala, I.,Williamson, M.P.,Lovering, A.L.,Mesnage, S.
Two-site recognition of Staphylococcus aureus peptidoglycan by lysostaphin SH3b.
Nat.Chem.Biol., 16:24-30, 2020
Cited by
PubMed Abstract: Lysostaphin is a bacteriolytic enzyme targeting peptidoglycan, the essential component of the bacterial cell envelope. It displays a very potent and specific activity toward staphylococci, including methicillin-resistant Staphylococcus aureus. Lysostaphin causes rapid cell lysis and disrupts biofilms, and is therefore a therapeutic agent of choice to eradicate staphylococcal infections. The C-terminal SH3b domain of lysostaphin recognizes peptidoglycans containing a pentaglycine crossbridge and has been proposed to drive the preferential digestion of staphylococcal cell walls. Here we elucidate the molecular mechanism underpinning recognition of staphylococcal peptidoglycan by the lysostaphin SH3b domain. We show that the pentaglycine crossbridge and the peptide stem are recognized by two independent binding sites located on opposite sides of the SH3b domain, thereby inducing a clustering of SH3b domains. We propose that this unusual binding mechanism allows synergistic and structurally dynamic recognition of S. aureus peptidoglycan and underpins the potent bacteriolytic activity of this enzyme.
PubMed: 31686030
DOI: 10.1038/s41589-019-0393-4
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.43 Å)
構造検証レポート
Validation report summary of 6rk4
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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