Abstract
The Sec complex forms the core of a conserved machinery transporting proteins across or into membranes. In
Escherichia coli SecYEG is active as an oligomer, but the structure predicts that the protein-conducting channel is formed by the monomer. A homology model of the
E.
coli
complex was built using the atomic structure of
Methanococcus jannaschii SecYEβ. Another structure of the membrane-bound dimer was then determined by fitting the homology model to an 8
Å map of SecYEG determined by electron microscopy. We found that the substrate-binding site of the dimer has opened slightly and the plug domain moved toward the outside. This new position retains the channel in a closed state. These differences partially reflect the movements that have been proposed to occur during channel gating. Further opening of the substrate-binding pocket to bind and release bound substrate and displacement of the plug during secretion, presumably rely on the action of the partner proteins. The contacts arising at the dimer interface in the environment of the lipid bilayer may have activated the assembly.