Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy |
| |
Authors: | Chen Yong Pan Xijiang Tang Ying Quan Shu Tai Phang C Sui Sen-Fang |
| |
Institution: | ‡Department of Biological Sciences and Biotechnology, the State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China and the §Department of Biology, Georgia State University, Atlanta, Georgia 30303 |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|