Protein Translocation: SecA-SecY Conformational Crosstalk Opens Channel.

Curr Biol

Department of Chemistry and Biochemistry, The Ohio State University, 580 Bioscience, 484 West 12(th) Avenue, Columbus, OH 43210, USA. Electronic address:

Published: September 2016

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.

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Source
http://dx.doi.org/10.1016/j.cub.2016.07.010DOI Listing

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