Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
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葡萄球菌 LukF 的晶体结构描绘了伴随跨膜通道形成的构象变化
DOI：
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发表时间：
1999
期刊：
影响因子：
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通讯作者：
E. Gouaux
中科院分区：
文献类型：
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作者：
R. Olson;H. Nariya;K. Yokota;Y. Kamio;E. Gouaux
葡萄球菌LukF、LukS、HγII和α-溶血素是在序列和功能上相关的自组装、通道形成蛋白。在α-溶血素七聚体中，形成通道的β链和氨基闩锁从原聚体核心长距离移动。在这里，我们报告了LukF的水溶性形式的晶体结构。在LukF结构中，通道形成区折叠成两亲性的三链β折叠，并且氨基闩锁形成延伸中心β折叠的β链。LukF结构说明了通道形成毒素如何在细胞结合和组装之前掩蔽蛋白质-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的终点。
Staphylococcal LukF, LukS, HγII, and α–hemolysin are self–assembling, channel–forming proteins related in sequence and function. In the α–hemolysin heptamer, the channel–forming β–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 β–sheet and the amino latch forms a β–strand extending a central β–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 α–hemolysin heptamer structure, they define the end points on the pathway of toxin assembly.
影响因子：
56.9
作者：
HENDRICKSON, WA
通讯作者：
HENDRICKSON, WA