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Related Experiment Videos

Structural insight into the protein translocation channel.

William M Clemons1, Jean-François Ménétret, Christopher W Akey

  • 1Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.

Current Opinion in Structural Biology
|August 18, 2004
PubMed
Summary
This summary is machine-generated.

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The SecY complex forms a protein translocation channel. Structural studies reveal its pore allows protein passage across membranes and insertion into the lipid bilayer.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The SecY complex (and homologous Sec61 complex in eukaryotes) forms a conserved protein translocation channel essential for protein transport across cellular membranes.
  • Previous models proposed the channel functions as an oligomeric assembly.

Purpose of the Study:

  • To investigate the structural basis of protein translocation through the SecY complex.
  • To reconcile findings from electron microscopy and X-ray crystallography regarding SecY complex function.

Main Methods:

  • X-ray crystallography of archaeal SecY complex.
  • Electron microscopy studies of Sec61/SecY complexes.

Main Results:

  • The X-ray structure reveals the protein translocation pore is centrally located within a single SecY complex molecule.

Related Experiment Videos

  • The pore structure explains mechanisms for translocating secretory proteins and inserting membrane proteins.
  • Both electron microscopy and X-ray data suggest a single SecY/Sec61 complex translocates polypeptides at a time.

    • Conclusions:

    • The SecY/Sec61 complex functions as a monomeric channel for protein translocation.
    • Structural insights clarify the dual roles of the channel in protein transport and membrane protein biogenesis.