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3j01

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3j01, resolution 7.10Å ()
Related: 3j00


Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

Structure of the ribosome-SecYE complex in the membrane environment

Publication Abstract from PubMed

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.

Cryo-EM structure of the ribosome-SecYE complex in the membrane environment., Frauenfeld J, Gumbart J, Sluis EO, Funes S, Gartmann M, Beatrix B, Mielke T, Berninghausen O, Becker T, Schulten K, Beckmann R, Nat Struct Mol Biol. 2011 May;18(5):614-21. Epub 2011 Apr 17. PMID:21499241

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3j01 is a 33 chain structure with sequence from Escherichia coli 536, Escherichia coli dh1 and Escherichia coli k-12. Full crystallographic information is available from OCA.

See Also

Reference

  • Frauenfeld J, Gumbart J, Sluis EO, Funes S, Gartmann M, Beatrix B, Mielke T, Berninghausen O, Becker T, Schulten K, Beckmann R. Cryo-EM structure of the ribosome-SecYE complex in the membrane environment. Nat Struct Mol Biol. 2011 May;18(5):614-21. Epub 2011 Apr 17. PMID:21499241 doi:10.1038/nsmb.2026

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