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TitleArchitecture of the active post-translational Sec translocon.
Journal, issue, pagesEMBO J, Vol. 40, Issue 3, Page e105643, Year 2021
Publish dateFeb 1, 2021
AuthorsTsai-Hsuan Weng / Wieland Steinchen / Birgitta Beatrix / Otto Berninghausen / Thomas Becker / Gert Bange / Jingdong Cheng / Roland Beckmann /
PubMed AbstractIn eukaryotes, most secretory and membrane proteins are targeted by an N-terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein-conducting channel ...In eukaryotes, most secretory and membrane proteins are targeted by an N-terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein-conducting channel (PCC). In the post-translational mode, fully synthesized proteins are recognized by a specialized channel additionally containing the Sec62, Sec63, Sec71, and Sec72 subunits. Recent structures of this Sec complex in the idle state revealed the overall architecture in a pre-opened state. Here, we present a cryo-EM structure of the yeast Sec complex bound to a substrate, and a crystal structure of the Sec62 cytosolic domain. The signal sequence is inserted into the lateral gate of Sec61α similar to previous structures, yet, with the gate adopting an even more open conformation. The signal sequence is flanked by two Sec62 transmembrane helices, the cytoplasmic N-terminal domain of Sec62 is more rigidly positioned, and the plug domain is relocated. We crystallized the Sec62 domain and mapped its interaction with the C-terminus of Sec63. Together, we obtained a near-complete and integrated model of the active Sec complex.
External linksEMBO J / PubMed:33305433 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.54 - 4.4 Å
Structure data

11774

7aft

EMDB-11774, PDB-7aft:
Cryo-EM structure of the signal sequence-engaged post-translational Sec translocon
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-11775:
Cryo-EM structure of the apo state post-translational Sec translocon
Method: EM (single particle) / Resolution: 4.3 Å

PDB-6zzz:
Crystal structure of yeast Sec62 cytoplasmic domain
Method: X-RAY DIFFRACTION / Resolution: 2.54 Å

Chemicals

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM / MES (buffer)

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • Saccharomyces cerevisiae (brewer's yeast)
KeywordsPROTEIN TRANSPORT / Sec62 / Sec62 domain / Post translocon / MEMBRANE PROTEIN / Post-translational translocation / Protein translocation / Sec complex / Signal sequence

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