Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy.
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.
Chen
Yong
Y
Department of Biological Sciences and Biotechnology, the State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China.
Pan
Xijiang
X
Tang
Ying
Y
Quan
Shu
S
Tai
Phang C
PC
Sui
Sen-Fang
SF
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D020285:Cryoelectron Microscopy / Q000379:methods*; D019281:Dimerization; D004926:Escherichia coli / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry*; D008968:Molecular Conformation; D011487:Protein Conformation; D000069816:SEC Translocation Channels; D000081416:SecA Proteins; D055672:Static Electricity
D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D000069816:SEC Translocation Channels; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins
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