A molecular switch in SecA protein couples ATP hydrolysis to protein translocation.

@article{Karamanou1999AMS,
  title={A molecular switch in SecA protein couples ATP hydrolysis to protein translocation.},
  author={Spyridoula Karamanou and Eleftheria Vrontou and Georgios Sianidis and Catherine Baud and Tilmann Roos and Andreas Kuhn and A. S. Politou and Anastassios Economou},
  journal={Molecular microbiology},
  year={1999},
  volume={34 5},
  pages={1133-45}
}
SecA, the dimeric ATPase subunit of bacterial protein translocase, catalyses translocation during ATP-driven membrane cycling at SecYEG. We now show that the SecA protomer comprises two structural modules: the ATPase N-domain, containing the nucleotide binding sites NBD1 and NBD2, and the regulatory C-domain. The C-domain binds to the N-domain in each protomer and to the C-domain of another protomer to form SecA dimers. NBD1 is sufficient for single rounds of SecA ATP hydrolysis. Multiple ATP… CONTINUE READING

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