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5ABB

Visualization of a polytopic membrane protein during SecY-mediated membrane insertion

Summary for 5ABB
Entry DOI10.2210/pdb5abb/pdb
EMDB information2446
DescriptorPROTEIN TRANSLOCASE SUBUNIT SECY, PROTEIN TRANSLOCASE SUBUNIT SECE, GREEN-LIGHT ABSORBING PROTEORHODOPSIN (3 entities in total)
Functional Keywordstranslation, ribosome, membrane protein, translocon
Biological sourceESCHERICHIA COLI
More
Cellular locationCell inner membrane ; Multi-pass membrane protein . Membrane ; Multi-pass membrane protein : B7MCR5
Cell membrane ; Multi-pass membrane protein : Q9F7P4
Total number of polymer chains3
Total formula weight68811.35
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 citationBischoff, 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: 24912953
DOI: 10.1038/NCOMMS5103
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8 Å)
Structure validation

227344

数据于2024-11-13公开中

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