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

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50431

Mielke,  T.
Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-7890-C
Zusammenfassung
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.