2QK7

A covalent S-F heterodimer of staphylococcal gamma-hemolysin

2QK7 の概要

• エントリーDOI: 10.2210/pdb2qk7/pdb
• 関連するPDBエントリー: 1LKF 1PVL 1T5R 2LKF 3LKF
• 分子名称: Gamma-hemolysin component A, Gamma-hemolysin component B (3 entities in total)
• 機能のキーワード: pore-forming toxin, beta-barrel, protein-protein interaction, molecular plasticity, covalent complex, cytolysis, hemolysis, secreted, toxin
• 由来する生物種: Staphylococcus aureus subsp. aureus; 詳細
• 細胞内の位置: Secreted: P0A074
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67606.41

構造登録者

Roblin, P.,Guillet, V.,Maveyraud, L.,Mourey, L. (登録日: 2007-07-10, 公開日: 2008-02-19, 最終更新日: 2024-10-30)

主引用文献

Roblin, P.,Guillet, V.,Joubert, O.,Keller, D.,Erard, M.,Maveyraud, L.,Prevost, G.,Mourey, L.
A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins.
Proteins, 71:485-496, 2008

PubMed Abstract: Staphylococcal leucotoxins, leucocidins, and gamma-hemolysins are bicomponent beta-barrel pore-forming toxins (beta-PFTs). Their production is associated with several clinical diseases. They have cytotoxic activity due to the synergistic action of a class S component and a class F component, which are secreted as water-soluble monomers and form hetero-oligomeric transmembrane pores, causing the lysis of susceptible cells. Structural information is currently available for the monomeric S and F proteins and the homoheptamer formed by the related alpha-hemolysin. These structures illustrate the start and end points in the mechanistic framework of beta-PFT assembly. Only limited structural data exist for the intermediate stages, including hetero-oligomeric complexes of leucotoxins. We investigated the protein-protein interactions responsible for maintaining the final bipartite molecular architecture and describe here the high-resolution crystal structure and low-resolution solution structure of a site-specific cross-linked heterodimer of gamma-hemolysin (HlgA T28C-HlgB N156C), which were solved by X-ray crystallography and small angle X-ray scattering, respectively. These structures reveal a molecular plasticity of beta-PFTs, which may facilitate the transition from membrane-bound monomers to heterodimers.

PubMed: 18214982
DOI: 10.1002/prot.21900

実験手法

X-RAY DIFFRACTION (2.4 Å)