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  Structure of the native Sec61 protein-conducting channel

Pfeffer, S., Burbaum, L., Unverdorben, P., Pech, M., Chen, Y., Zimmermann, R., et al. (2015). Structure of the native Sec61 protein-conducting channel. NATURE COMMUNICATIONS, 6: 8403. doi:10.1038/ncomms9403.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-0A2D-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-0A2E-B
Genre: Journal Article

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 Creators:
Pfeffer, Stefan1, Author              
Burbaum, Laura1, Author              
Unverdorben, Pia1, Author              
Pech, Markus2, Author
Chen, Yuxiang1, Author              
Zimmermann, Richard2, Author
Beckmann, Roland2, Author
Förster, Friedrich1, Author              
Affiliations:
1Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              
2external, ou_persistent22              

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Free keywords: ENDOPLASMIC-RETICULUM; IN-SITU; CRYOELECTRON TOMOGRAPHY; ANGSTROM RESOLUTION; BACTERIAL TRANSLOCON; MOLECULAR-DYNAMICS; RIBOSOME BINDING; MEMBRANE; INSERTION; COMPLEX
 Abstract: In mammalian cells, secretory and membrane proteins are translocated across or inserted into the endoplasmic reticulum (ER) membrane by the universally conserved protein-conducting channel Sec61, which has been structurally studied in isolated, detergent-solubilized states. Here we structurally and functionally characterize native, non-solubilized ribosome-Sec61 complexes on rough ER vesicles using cryo-electron tomography and ribosome profiling. Surprisingly, the 9-angstrom resolution subtomogram average reveals Sec61 in a laterally open conformation, even though the channel is not in the process of inserting membrane proteins into the lipid bilayer. In contrast to recent mechanistic models for polypeptide translocation and insertion, our results indicate that the laterally open conformation of Sec61 is the only conformation present in the ribosome-bound translocon complex, independent of its functional state. Consistent with earlier functional studies, our structure suggests that the ribosome alone, even without a nascent chain, is sufficient for lateral opening of Sec61 in a lipid environment.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published online
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000363137700003
DOI: 10.1038/ncomms9403
 Degree: -

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Title: NATURE COMMUNICATIONS
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 6 Sequence Number: 8403 Start / End Page: - Identifier: ISSN: 2041-1723