通过冷冻电子显微镜确定，全长大肠杆菌SecA在溶液中以封闭构象二聚化。
Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy.
作者信息
Chen Yong, Pan Xijiang, Tang Ying, Quan Shu, Tai Phang C, Sui Sen-Fang
机构信息
Department of Biological Sciences and Biotechnology, the State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China.
出版信息
J Biol Chem. 2008 Oct 24;283(43):28783-7. doi: 10.1074/jbc.C800160200. Epub 2008 Sep 4.
Abstract
SecA is an obligatory component of the Escherichia coli general secretion pathway. However, the oligomeric structure of SecA and SecA conformational changes during translocation processes are still unclear. Here we obtained the three-dimensional structure of E. coli wild-type full-length SecA in solution by single particle cryo-electron microscopy and determined its oligomeric organization. In this structure, SecA occurs as a dimer in which the two protomers are arranged in an antiparallel mode, with a novel electrostatic interface, and both protomers are in closed conformation. The system developed here may provide a promising technique for studying dynamic structural changes in SecA.
摘要
SecA是大肠杆菌通用分泌途径的一个必需组成部分。然而，SecA的寡聚结构以及转运过程中SecA的构象变化仍不清楚。在这里，我们通过单颗粒冷冻电子显微镜获得了溶液中大肠杆菌野生型全长SecA的三维结构，并确定了其寡聚组织。在这个结构中，SecA以二聚体形式存在，其中两个原体以反平行模式排列，具有一个新的静电界面，并且两个原体都处于封闭构象。这里开发的系统可能为研究SecA的动态结构变化提供一种有前景的技术。
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