Ontology highlight
ABSTRACT:
SUBMITTER: Frauenfeld J
PROVIDER: S-EPMC3412285 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Frauenfeld Jens J Gumbart James J Sluis Eli O van der EO Funes Soledad S Gartmann Marco M Beatrix Birgitta B Mielke Thorsten T Berninghausen Otto O Becker Thomas T Schulten Klaus K Beckmann Roland R
Nature structural & molecular biology 20110417 5
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 polypept ...[more]