Sign up & Download
Sign in

Simulations of a protein translocation pore: SecY

by Shozeb Haider, Benjamin A. Hall, M. S P Sansom
Biochemistry ()


SecY is the central channel protein of the SecYEbeta translocon, the structure of which has been determined by X-ray diffraction. Extended (15 ns) MD simulations of the isolated SecY protein in a phospholipid bilayer have been performed to explore the relationship between protein flexibility and the mechanisms of channel gating. In particular, principal components analysis of the simulation trajectory has been used to probe the intrinsic flexibility of the isolated SecY protein in the absence of the gamma-subunit (SecE) clamp. Analysis and visualization of the principal eigenvectors support a "plug and clamshell" model of SecY channel gating. The simulation results also indicate that hydrophobic gating at the central pore ring prevents leakage of water and ions through the channel in the absence of a translocating peptide.

Cite this document (BETA)

Authors on Mendeley

Readership Statistics

25 Readers on Mendeley
by Discipline
by Academic Status
32% Post Doc
28% Ph.D. Student
4% Student (Bachelor)
by Country
12% United States
8% United Kingdom
4% Portugal


Sign up today - FREE

Mendeley saves you time finding and organizing research. Learn more

  • All your research in one place
  • Add and import papers easily
  • Access it anywhere, anytime

Start using Mendeley in seconds!

Sign up & Download

Already have an account? Sign in