Jens Frauenfeld 1 , 2 , James Gumbart 3 , Eli O. van Sluis 1 , 2 , Soledad Funes 4 , Marco Gartmann 1 , 2 , Birgitta Beatrix 1 , 2 , Thorsten Mielke 5 , Otto Berninghausen 1 , 2 , Thomas Becker 1 , 2 , Klaus Schulten 3 , Roland Beckmann 1 , 2 , #
17 April 2011
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–electron microscopy structure of the SecYEG complex in a membrane environment at sub–nanometer resolution, bound to a translating ribosome. Using the SecYEG complex reconstituted in a so–called Nanodisc, we could trace the nascent polypeptide chain from the peptidyl transferase 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 PCC. Based on our map and molecular dynamics simulations we present a model of a signal anchor–gated PCC in the membrane.