4CT3
Methylmercury chloride derivative structure of the lytic CHAPK domain of the endolysin LysK from Staphylococcus aureus bacteriophage K
4CT3 の概要
| エントリーDOI | 10.2210/pdb4ct3/pdb |
| 関連するPDBエントリー | 4CSH |
| 分子名称 | ORF30/ORF32, CHLORIDE ION, GLYCEROL, ... (8 entities in total) |
| 機能のキーワード | viral protein, peptidoglycan, protease |
| 由来する生物種 | Kayvirus kay |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 79598.92 |
| 構造登録者 | Sanz-Gaitero, M.,Keary, R.,Garcia-Doval, C.,Coffey, A.,van Raaij, M.J. (登録日: 2014-03-12, 公開日: 2014-08-06, 最終更新日: 2024-11-20) |
| 主引用文献 | Sanz-Gaitero, M.,Keary, R.,Garcia-Doval, C.,Coffey, A.,van Raaij, M.J. Crystal structure of the lytic CHAP(K) domain of the endolysin LysK from Staphylococcus aureus bacteriophage K. Virol. J., 11:133-133, 2014 Cited by PubMed Abstract: Bacteriophages encode endolysins to lyse their host cell and allow escape of their progeny. Endolysins are also active against Gram-positive bacteria when applied from the outside and are thus attractive anti-bacterial agents. LysK, an endolysin from staphylococcal phage K, contains an N-terminal cysteine-histidine dependent amido-hydrolase/peptidase domain (CHAP(K)), a central amidase domain and a C-terminal SH3b cell wall-binding domain. CHAP(K) cleaves bacterial peptidoglycan between the tetra-peptide stem and the penta-glycine bridge. PubMed: 25064136DOI: 10.1186/1743-422X-11-133 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.69 Å) |
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