4V6M
Structure of the ribosome-SecYE complex in the membrane environment
This is a non-PDB format compatible entry.
Summary for 4V6M
| Entry DOI | 10.2210/pdb4v6m/pdb |
| EMDB information | 1858 |
| Descriptor | 16S RIBOSOMAL RNA, 30S ribosomal protein S6, 30S ribosomal protein S7, ... (61 entities in total) |
| Functional Keywords | ribosomal protein, ribonucleoprotein, nucleotide-binding, protein biosynthesis, translation, zinc-finger, 70s ribosome, ribosome, translocon, secyeg, nanodisc, ribosome-ribosomal protein complex, ribosome/ribosomal protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 60 |
| Total formula weight | 2410929.31 |
| Authors | Frauenfeld, J.,Gumbart, J.,van der Sluis, E.O.,Funes, S.,Gartmann, M.,Beatrix, B.,Mielke, T.,Berninghausen, O.,Becker, T.,Schulten, K.,Beckmann, R. (deposition date: 2011-02-08, release date: 2014-07-09, Last modification date: 2024-02-28) |
| Primary citation | Frauenfeld, J.,Gumbart, J.,Sluis, E.O.,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., 18:614-621, 2011 Cited by PubMed 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. PubMed: 21499241DOI: 10.1038/nsmb.2026 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.1 Å) |
Structure validation
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