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  Atomic Model of the E. coli Membrane-bound Protein Translocation Complex SecYEG

Bostina, M., Mohsin, B., Kühlbrandt, W., & Collinson, I. (2005). Atomic Model of the E. coli Membrane-bound Protein Translocation Complex SecYEG. Journal of Molecular Biology (London), 352(5), 1035-1043. doi:10.1016/j.jmb.2005.08.005.

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 Creators:
Bostina, Mihnea1, Author           
Mohsin, Brigitte1, Author           
Kühlbrandt, Werner1, Author           
Collinson, Ian1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: protein translocation; structure; model; membrane-bound; conformational changes
 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.

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Language(s): eng - English
 Dates: 2005-08-032005-06-082005-08-032005-05-242005-10-07
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jmb.2005.08.005
PMID: 16154141
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 352 (5) Sequence Number: - Start / End Page: 1035 - 1043 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042