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TitleStructure of the posttranslational Sec protein-translocation channel complex from yeast.
Journal, issue, pagesScience, Vol. 363, Issue 6422, Page 84-87, Year 2019
Publish dateJan 4, 2019
AuthorsSamuel Itskanov / Eunyong Park /
PubMed AbstractThe Sec61 protein-conducting channel mediates transport of many proteins, such as secretory proteins, across the endoplasmic reticulum (ER) membrane during or after translation. Posttranslational ...The Sec61 protein-conducting channel mediates transport of many proteins, such as secretory proteins, across the endoplasmic reticulum (ER) membrane during or after translation. Posttranslational transport is enabled by two additional membrane proteins associated with the channel, Sec63 and Sec62, but its mechanism is poorly understood. We determined a structure of the Sec complex (Sec61-Sec63-Sec71-Sec72) from by cryo-electron microscopy (cryo-EM). The structure shows that Sec63 tightly associates with Sec61 through interactions in cytosolic, transmembrane, and ER-luminal domains, prying open Sec61's lateral gate and translocation pore and thus activating the channel for substrate engagement. Furthermore, Sec63 optimally positions binding sites for cytosolic and luminal chaperones in the complex to enable efficient polypeptide translocation. Our study provides mechanistic insights into eukaryotic posttranslational protein translocation.
External linksScience / PubMed:30545845 / PubMed Central
MethodsEM (single particle)
Resolution3.68 Å
Structure data

0336

6n3q

EMDB-0336, PDB-6n3q:
Cryo-EM structure of the yeast Sec complex
Method: EM (single particle) / Resolution: 3.68 Å

Source
  • Saccharomyces cerevisiae S288c (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsTRANSPORT PROTEIN / Sec61 / Sec63 / Sec71 / Sec72 / Sec66 / protein translocation / translocon / endoplasmic reticulum / secretion

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