Structure of the outer membrane complex of a type IV secretion system.

Structure of the outer membrane complex of a type IV secretion system.
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DOI:
10.1038/nature08588
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发表时间:
2009-12-24
期刊:
影响因子:
64.8
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--
中科院分区:
综合性期刊1区
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IV型分泌系统是跨越革兰氏阴性细菌两层膜的分泌纳米机器。三种蛋白质,VirB7,VirB9和VirB10组装成一个1.05的丙二醛核心,横跨内膜和外膜。这个核心由每个蛋白质的14个拷贝组成,形成两层,分别插入内膜和外膜,即I层和O层。在这里,我们提出了一个~0.6丙二醛外膜络合物的晶体结构,包含了整个O层。这个结构是外膜通道中确定的最大结构,也是史无前例的由三种蛋白质组成的结构。出乎意料的是,这一结构将VirB10确定为具有独特疏水双螺旋跨膜区的外膜通道。这种结构使VirB10成为唯一已知的跨越革兰氏阴性细菌两层膜的蛋白质。低温电子显微镜和结晶学结构的比较表明,构象变化调节着通道的开启和关闭。
Type IV secretion systems are secretion nanomachines spanning the two membranes of Gram-negative bacteria. Three proteins, VirB7, VirB9, and VirB10 assemble into a 1.05 MDa core spanning the inner and outer membranes. This core consists of 14 copies of each of the proteins and forms two layers, the I and O layers, inserting in the inner and outer membrane, respectively. Here we present the crystal structure of a ~0.6 MDa outer membrane complex containing the entire O-layer. This structure is the largest determined for an outer membrane channel and is also unprecedented in being composed of three proteins. Unexpectedly, this structure identifies VirB10 as the outer membrane channel with a unique hydrophobic double helical trans-membrane region. This structure establishes VirB10 as the only known protein crossing both membranes of Gram-negative bacteria. Comparison of the cryo-EM and crystallographic structures point to conformational changes regulating channel opening and closing.
革兰氏阴性细菌中非flagellar蛋白附加的结构和生物发生。
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发表时间: 2009-10
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影响因子: --
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