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  Cryo-EM structure of the ribosome-SecYE complex in the membrane environment

Frauenfeld, J., Gumbart, J., Sluis, E. O., Funes, S., Gartmann, M., Beatrix, B., et al. (2011). Cryo-EM structure of the ribosome-SecYE complex in the membrane environment. Nature Structural & Molecular Biology, 18(5), 614-21. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/21499241 http://www.nature.com/nsmb/journal/v18/n5/pdf/nsmb.2026.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7890-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7891-A
Genre: Journal Article

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Frauenfeld, J., Author
Gumbart, J., Author
Sluis, E. O., Author
Funes, S., Author
Gartmann, M., Author
Beatrix, B., Author
Mielke, T.1, Author              
Berninghausen, O., Author
Becker, T., Author
Schulten, K., Author
Beckmann, R., Author
Affiliations:
1Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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Free keywords: Cell Membrane/*metabolism; Cryoelectron Microscopy; Escherichia coli; Escherichia coli Proteins/*chemistry/metabolism; Lipoproteins, HDL/chemistry/metabolism; Membrane Proteins/*chemistry/metabolism; Models, Molecular; Protein Transport; Ribosomes/*chemistry; Signal Recognition Particle/physiology
 Abstract: The ubiquitous SecY-Sec61 complex translocates nascent secretory proteins across cellular membranes and integrates membrane proteins into lipid bilayers. Several structures of mostly detergent-solubilized Sec complexes have been reported. Here we present a single-particle cryo-EM structure of the SecYEG complex in a membrane environment, bound to a translating ribosome, at subnanometer resolution. Using the SecYEG complex reconstituted in a so-called Nanodisc, we could trace the nascent polypeptide chain from the peptidyltransferase center into the membrane. The reconstruction allowed for the identification of ribosome-lipid interactions. The rRNA helix 59 (H59) directly contacts the lipid surface and appears to modulate the membrane in immediate vicinity to the proposed lateral gate of the protein-conducting channel (PCC). On the basis of our map and molecular dynamics simulations, we present a model of a signal anchor-gated PCC in the membrane.

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 Dates: 2011
 Publication Status: Published in print
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Title: Nature Structural & Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 18 (5) Sequence Number: - Start / End Page: 614 - 21 Identifier: ISSN: 1545-9985 (Electronic) 1545-9985 (Linking)