PMID:21499241
| Citation |
Frauenfeld, J, Gumbart, J, Sluis, EO, Funes, S, Gartmann, M, Beatrix, B, Mielke, T, Berninghausen, O, Becker, T, Schulten, K and Beckmann, R (2011) Cryo-EM structure of the ribosome-SecYE complex in the membrane environment. Nat. Struct. Mol. Biol. 18:614-21 |
|---|---|
| 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. |
| Links |
PubMed PMC3412285 Online version:10.1038/nsmb.2026 |
| Keywords |
Cell Membrane/metabolism; Cryoelectron Microscopy; Escherichia coli; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Lipoproteins, HDL/chemistry; Lipoproteins, HDL/metabolism; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Models, Molecular; Protein Transport; Ribosomes/chemistry; Signal Recognition Particle/physiology |
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