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Biophys. J. BioFAST: First Published January 13, 2006. doi:10.1529/biophysj.105.075291
© 2006 by the Biophysical Society.

A more recent version of this article appeared on April 1, 2006.
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CHANNELS, RECEPTORS, AND ELECTRICAL SIGNALING

Molecular dynamics studies of the archaeal translocon

James C. Gumbart 1 and Klaus Schulten 2*

1 University of Illinois, Urbana-Champaign
2 University of Illinois 3143 Beckman Institute

* To whom correspondence should be addressed. E-mail: kschulte{at}ks.uiuc.edu.

Submitted on October 5, 2005
Revised on November 8, 2005
Accepted on 19 December 2005


  Abstract
The translocon is a protein-conducting channel conserved over all domains of life that serves to translocate proteins across or into membranes. While this channel has been well-studied for many years, the recent discovery of a high-resolution crystal structure opens up new avenues of exploration. Taking advantage of this, we performed molecular dynamics simulations of the translocon in a fully-solvated lipid bilayer, examining the translocation abilities of monomeric SecYE{beta} by forcing two helices comprised of different amino acid sequences to cross the channel. The simulations revealed that the so-called `plug' of SecYE{beta} swings open during translocation, closing thereafter. Likewise, it was established that the so-called `pore ring' region of SecYE{beta} forms an elastic, yet tight seal around the translocating oligopeptides. The closed state of the channel was found to block permeation of all ions and water molecules; in the open state, ions were blocked. Our results suggest that the SecYE{beta} monomer is capable of forming an active channel.

Key Words: SecY, membrane proteins, simulation, translocation




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Copyright © 2006 by the Biophysical Society.