Protein Translocation: SecA-SecY Conformational Crosstalk Opens Channel.
A new study of the bacterial Sec translocase complex reports that ADP/ATP binding to SecA triggers multiple conformational changes in the SecYEG channel that may allow the passive directional movement of the polypeptide chain.
Institute of Microbiology and Molecular Biology, University of Hohenheim, 70599 Stuttgart, Germany. Electronic address: Andreas.Kuhn@uni-hohenheim.de.
Andreas
A
Kuhn
Department of Chemistry and Biochemistry, The Ohio State University, 580 Bioscience, 484 West 12(th) Avenue, Columbus, OH 43210, USA. Electronic address: dalbey.1@osu.edu.
Ross E
RE
Dalbey
D000251:Adenosine Triphosphatases; D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D021381:Protein Transport; D000069816:SEC Translocation Channels
D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D000069816:SEC Translocation Channels; D000251:Adenosine Triphosphatases