Structure of the SecY channel during initiation of protein translocation

Eunyong Park, Jean-François Ménétret, James C. Gumbart, Steven J. Ludtke, Weikai Li, Andrew Whynot, Tom A. Rapoport () and Christopher W. Akey ()
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Eunyong Park: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Jean-François Ménétret: Boston University School of Medicine, 700 Albany Street, Boston, Massachusetts 02118-2526, USA
James C. Gumbart: School of Physics, Georgia Institute of Technology
Steven J. Ludtke: National Center for Macromolecular Imaging, Baylor College of Medicine, 1 Baylor Plaza, Houston, Texas 77030, USA
Weikai Li: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Andrew Whynot: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Tom A. Rapoport: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Christopher W. Akey: Boston University School of Medicine, 700 Albany Street, Boston, Massachusetts 02118-2526, USA

Nature, 2014, vol. 506, issue 7486, 102-106

Abstract: Newly synthesized proteins are targeted to the SecY protein-conducting channel for translocation across the membrane; here, cryo-electron microscopy structures of inactive and active ribosome–channel complexes are presented, revealing that ribosome binding does not result in major structural changes to transmembrane regions of the channel, and that stable channel opening requires loop insertion of the translocating nascent chain.

Date: 2014
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DOI: 10.1038/nature12720

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