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TitleStructure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation.
Journal, issue, pagesScience, Vol. 359, Issue 6375, Page 545-550, Year 2018
Publish dateFeb 2, 2018
AuthorsRebekka Wild / Julia Kowal / Jillianne Eyring / Elsy M Ngwa / Markus Aebi / Kaspar P Locher /
PubMed AbstractOligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to ...Oligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to glycosylation sites of secretory proteins. Here we describe the atomic structure of yeast OST determined by cryo-electron microscopy, revealing a conserved subunit arrangement. The active site of the catalytic STT3 subunit points away from the center of the complex, allowing unhindered access to substrates. The dolichol-pyrophosphate moiety binds to a lipid-exposed groove of STT3, whereas two noncatalytic subunits and an ordered N-glycan form a membrane-proximal pocket for the oligosaccharide. The acceptor polypeptide site faces an oxidoreductase domain in stand-alone OST complexes or is immediately adjacent to the translocon, suggesting how eukaryotic OSTs efficiently glycosylate a large number of polypeptides before their folding.
External linksScience / PubMed:29301962
MethodsEM (single particle)
Resolution3.4 Å
Structure data

EMDB-4257:
Additional yeast OST cryoEM maps from focused 3D refinements
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • Saccharomyces (fungus)

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