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  A structural model of the active ribosome-bound membrane protein insertase YidC.

Wickles, S., Singharoy, A., Andreani, J., Seemayer, S., Bischoff, L., Berninghausen, O., et al. (2014). A structural model of the active ribosome-bound membrane protein insertase YidC. eLife, 3: e03035. doi:10.7554/eLife.03035.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-001A-26A6-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-6DE2-F
Genre: Journal Article

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 Creators:
Wickles, S., Author
Singharoy, A., Author
Andreani, J.1, Author              
Seemayer, S., Author
Bischoff, L., Author
Berninghausen, O., Author
Söding, J.1, Author              
Schulten, K., Author
van der Sluis, E. O., Author
Beckmann, R., Author
Affiliations:
1Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              

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 Abstract: The integration of most membrane proteins into the cytoplasmic membrane of bacteria occurs co-translationally. The universally conserved YidC protein mediates this process either individually as a membrane protein insertase, or in concert with the SecY complex. Here, we present a structural model of YidC based on evolutionary co-variation analysis, lipid-versus-protein-exposure and molecular dynamics simulations. The model suggests a distinctive arrangement of the conserved five transmembrane domains and a helical hairpin between transmembrane segment 2 (TM2) and TM3 on the cytoplasmic membrane surface. The model was used for docking into a cryo-electron microscopy reconstruction of a translating YidC-ribosome complex carrying the YidC substrate FOc. This structure reveals how a single copy of YidC interacts with the ribosome at the ribosomal tunnel exit and identifies a site for membrane protein insertion at the YidC protein-lipid interface. Together, these data suggest a mechanism for the co-translational mode of YidC-mediated membrane protein insertion.

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Language(s): eng - English
 Dates: 2014-07-10
 Publication Status: Published online
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.03035
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Title: eLife
Source Genre: Journal
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Pages: 17 Volume / Issue: 3 Sequence Number: e03035 Start / End Page: - Identifier: -