Aerolysin - A paradigm for membrane insertion of beta-sheet protein toxins?
Aerolysin - A paradigm for membrane insertion of beta-sheet protein toxins?
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DOI：
10.1006/jsbi.1997.3947
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发表时间：
1998-01-01
影响因子：
3
通讯作者：
Parker, MW
中科院分区：
文献类型：
--
作者：
Rossjohn, J;Feil, SC;Parker, MW
细菌蛋白质气溶素原的晶体结构的测定提供了主要由β-折叠构建的成孔毒素的第一个视图。所获得的结构和随后的晶体学和生物化学研究一起使我们能够解释毒素是如何从水溶性二聚体转化为七聚体跨膜孔的。气溶素和其他毒素之间的结构相似性的最新发现表明，我们所做的结构/功能的研究可能被证明是有用的，在了解一些孔形成蛋白的行动。(C)北京：科学出版社.
The determination of the crystal structure of the bacterial protein proaerolysin provided the first view of a pore-forming toxin constructed mainly from beta-sheet. The structure that was obtained and subsequent crystallographic and biochemical studies have together allowed us to explain how the toxin is transformed from a water-soluble dimer to a heptameric transmembrane pore. Recent discoveries of structural similarities between aerolysin and other toxins suggest that the structure/function studies we have made may prove useful in understanding the actions of a number of pore-forming proteins. (C) 1998 Academic Press.