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潘顿-瓦伦丁杀白细胞素F组分的晶体结构

Crystal structure of the F component of the Panton-Valentine leucocidin.

作者信息

Pédelacq J D, Prévost G, Monteil H, Mourey L, Samama J P

机构信息

Groupe de Cristallographie Biologique, Institut de Pharmacologie et de Biologie Structurale du CNRS, Toulouse, France.

出版信息

Int J Med Microbiol. 2000 Oct;290(4-5):395-401. doi: 10.1016/S1438-4221(00)80050-8.

Abstract

Leucocidins and gamma-hemolysins are bi-component staphylococcal toxins that form lytic transmembrane pores. Their cytotoxic activities involve the synergistic association of a class S and a class F component, produced as water-soluble monomers which assemble on the surface of specific cells. The structure of the F protein from Panton-Valentine leucocidin, solved at 2.0 A resolution, and sequence alignment suggest that it represents the fold of any secreted protein in this family of toxins. The comparison of this structure to that of the homoheptameric alpha-hemolysin provides some insights into the molecular events that may occur during pore formation.

摘要

白细胞毒素和γ-溶血素是双组分葡萄球菌毒素,可形成溶解性跨膜孔道。它们的细胞毒性活性涉及S类和F类组分的协同结合,这些组分以水溶性单体形式产生,在特定细胞表面组装。以2.0埃分辨率解析的潘顿-瓦伦丁白细胞毒素F蛋白的结构以及序列比对表明,它代表了该毒素家族中任何分泌蛋白的折叠形式。将该结构与同七聚体α-溶血素的结构进行比较,为孔道形成过程中可能发生的分子事件提供了一些见解。

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