Structure of a bacterial type IV secretion core complex at subnanometre resolution.

Structure of a bacterial type IV secretion core complex at subnanometre resolution.
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DOI:
10.1038/emboj.2013.58
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发表时间:
2013-04-17
期刊:
影响因子:
11.4
通讯作者:
Orlova, Elena V.
Orlova, Elena V.
中科院分区:
生物学1区
文献类型:
--
作者:
Rivera-Calzada, Angel;Fronzes, Remi;Savva, Christos G.;Chandran, Vidya;Lian, Pei W.;Laeremans, Toon;Pardon, Els;Steyaert, Jan;Remaut, Han;Waksman, Gabriel;Orlova, Elena V.

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IV型分泌(T4s)系统能够通过细菌的膜运输DNA和/或蛋白质。它们形成由12种蛋白质组成的大型多蛋白复合体,称为VirB1-11和VirD4。VirB7、9和10组装成一个1.07百万吨的跨膜核心复合体(CC),所有其他组件都围绕着CC组装。这种复合体由两部分组成,即插入外膜的O层和插入内膜的I层。虽然X-射线结晶学已经解决了O-层的结构,但关于I-层的详细结构信息还没有。利用高分辨率低温电子显微镜和分子模拟结合生物化学方法,我们确定了I-层的结构,并在电子密度中定位了它的各种成分。我们的结果提供了关于CC的新的结构见解,从中可以推导出T4S系统机制的本质特征。
Type IV secretion (T4S) systems are able to transport DNAs and/or proteins through the membranes of bacteria. They form large multiprotein complexes consisting of 12 proteins termed VirB1-11 and VirD4. VirB7, 9 and 10 assemble into a 1.07 MegaDalton membrane-spanning core complex (CC), around which all other components assemble. This complex is made of two parts, the O-layer inserted in the outer membrane and the I-layer inserted in the inner membrane. While the structure of the O-layer has been solved by X-ray crystallography, there is no detailed structural information on the I-layer. Using high-resolution cryo-electron microscopy and molecular modelling combined with biochemical approaches, we determined the I-layer structure and located its various components in the electron density. Our results provide new structural insights on the CC, from which the essential features of T4S system mechanisms can be derived.
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