Olson R, Nariya H, Yokota K, Kamio Y, Gouaux E
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA.
Nat Struct Biol. 1999 Feb;6(2):134-40. doi: 10.1038/5821.
Staphylococcal LukF, LukS, HgammaII, and alpha-hemolysin are self-assembling, channel-forming proteins related in sequence and function. In the alpha-hemolysin heptamer, the channel-forming beta-strands and the amino latch make long excursions from the protomer core. Here we report the crystal structure of the water soluble form of LukF. In the LukF structure the channel-forming region folds into an amphipathic, three-strand beta-sheet and the amino latch forms a beta-strand extending a central beta-sheet. The LukF structure illustrates how a channel-forming toxin masks protein-protein and protein-membrane interfaces prior to cell binding and assembly, and together with the alpha-hemolysin heptamer structure, they define the end points on the pathway of toxin assembly.
葡萄球菌LukF、LukS、HgammaII和α-溶血素是在序列和功能上相关的自组装、形成通道的蛋白质。在α-溶血素七聚体中，形成通道的β链和氨基锁从原体核心处有较长的延伸。在此，我们报道了LukF水溶性形式的晶体结构。在LukF结构中，形成通道的区域折叠成一个两亲性的三链β-折叠片，氨基锁形成一条延伸中央β-折叠片的β链。LukF结构说明了一种形成通道的毒素在细胞结合和组装之前如何掩盖蛋白质-蛋白质和蛋白质-膜界面，并且与α-溶血素七聚体结构一起，它们定义了毒素组装途径上的端点。
