Structural insight into the protein translocation channel.
A structurally conserved protein translocation channel is formed by the heterotrimeric Sec61 complex in eukaryotes, and SecY complex in archaea and bacteria. Electron microscopy studies suggest that the channel may function as an oligomeric assembly of Sec61 or SecY complexes. Remarkably, the recently determined X-ray structure of an archaeal SecY complex indicates that the pore is located at the center of a single molecule of the complex. This structure suggests how the pore opens perpendicular to the plane of the membrane to allow the passage of newly synthesized secretory proteins across the membrane and opens laterally to allow transmembrane segments of nascent membrane proteins to enter the lipid bilayer. The electron microscopy and X-ray results together suggest that only one copy of the SecY or Sec61 complex within an oligomer translocates a polypeptide chain at any given time.
Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
William M
WM
Clemons
Jean-François
JF
Ménétret
Christopher W
CW
Akey
Tom A
TA
Rapoport
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D007473:Ion Channels / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D021381:Protein Transport / Q000502:physiology; D012270:Ribosomes / Q000378:metabolism; D000069816:SEC Translocation Channels; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D007473:Ion Channels; D008565:Membrane Proteins; D000069816:SEC Translocation Channels