5ABB
Visualization of a polytopic membrane protein during SecY-mediated membrane insertion
Summary for 5ABB
Entry DOI | 10.2210/pdb5abb/pdb |
EMDB information | 2446 |
Descriptor | PROTEIN TRANSLOCASE SUBUNIT SECY, PROTEIN TRANSLOCASE SUBUNIT SECE, GREEN-LIGHT ABSORBING PROTEORHODOPSIN (3 entities in total) |
Functional Keywords | translation, ribosome, membrane protein, translocon |
Biological source | ESCHERICHIA COLI More |
Cellular location | Cell inner membrane ; Multi-pass membrane protein . Membrane ; Multi-pass membrane protein : B7MCR5 Cell membrane ; Multi-pass membrane protein : Q9F7P4 |
Total number of polymer chains | 3 |
Total formula weight | 68811.35 |
Authors | Bischoff, L.,Wickles, S.,Berninghausen, O.,vanderSluis, E.,Beckmann, R. (deposition date: 2015-08-05, release date: 2015-08-19, Last modification date: 2024-05-08) |
Primary citation | Bischoff, L.,Wickles, S.,Berninghausen, O.,Van Der Sluis, E.O.,Beckmann, R. Visualization of a Polytopic Membrane Protein During Secy-Mediated Membrane Insertion. Nat.Commun., 5:4103-, 2014 Cited by PubMed Abstract: The biogenesis of polytopic membrane proteins occurs co-translationally on ribosomes that are tightly bound to a membrane-embedded protein-conducting channel: the Sec-complex. The path that is followed by nascent proteins inside the ribosome and the Sec-complex is relatively well established; however, it is not clear what the fate of the N-terminal transmembrane domains (TMDs) of polytopic membrane proteins is when the C-terminal TMDs domains are not yet synthesized. Here, we present the sub-nanometer cryo-electron microscopy structure of an in vivo generated ribosome-SecY complex that carries a membrane insertion intermediate of proteorhodopsin (PR). The structure reveals a pre-opened Sec-complex and the first two TMDs of PR already outside the SecY complex directly in front of its proposed lateral gate. Thus, our structure is in agreement with positioning of N-terminal TMDs at the periphery of SecY, and in addition, it provides clues for the molecular mechanism underlying membrane protein topogenesis. PubMed: 24912953DOI: 10.1038/NCOMMS5103 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8 Å) |
Structure validation
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