产肠毒素大肠杆菌2型分泌系统中GspK-GspI-GspJ复合物的结构
Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system.
作者信息
Korotkov Konstantin V, Hol Wim G J
机构信息
Department of Biochemistry, Biomolecular Structure Center, University of Washington, Box 357742, Seattle, Washington 98195, USA.
出版信息
Nat Struct Mol Biol. 2008 May;15(5):462-8. doi: 10.1038/nsmb.1426. Epub 2008 Apr 27.
Gram-negative bacteria translocate various proteins including virulence factors across their outer membrane via type 2 secretion systems (T2SSs). T2SSs are thought to contain a pseudopilus, a subcomplex formed by one major and several minor pseudopilins. We report the crystal structure of the complex formed by three minor pseudopilins from enterotoxigenic Escherichia coli. The GspK-GspI-GspJ complex has quasihelical characteristics and an architecture consistent with a localization at the pseudopilus tip. The alpha-domain of GspK has a previously unobserved fold with an unexpected dinuclear metal binding site. The area surrounding its disulfide bridge is conserved and might interact with other T2SS components or with secreted proteins.
革兰氏阴性菌通过2型分泌系统（T2SSs）将包括毒力因子在内的各种蛋白质转运穿过其外膜。T2SSs被认为包含一个假菌毛，它是由一种主要假菌毛蛋白和几种次要假菌毛蛋白形成的亚复合物。我们报道了产肠毒素大肠杆菌的三种次要假菌毛蛋白形成的复合物的晶体结构。GspK-GspI-GspJ复合物具有准螺旋特征，其结构与定位在假菌毛尖端一致。GspK的α结构域具有以前未观察到的折叠，带有一个意想不到的双核金属结合位点。其二硫键周围的区域是保守的，可能与其他T2SS成分或分泌蛋白相互作用。
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