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The Journal of Biological Chemistry
Year: 2008  |  Volume: 283  |  Issue: 43  |  Page No.: 28783 - 28787

Full-length Escherichia coli SecA Dimerizes in a Closed Conformation in Solution as Determined by Cryo-electron Microscopy

Yong Chen, Xijiang Pan, Ying Tang, Shu Quan, Phang C. Tai and Sen-Fang Sui    

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.

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