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TitleThe atomic structure of a eukaryotic oligosaccharyltransferase complex.
Journal, issue, pagesNature, Vol. 555, Issue 7696, Page 328-333, Year 2018
Publish dateMar 15, 2018
AuthorsLin Bai / Tong Wang / Gongpu Zhao / Amanda Kovach / Huilin Li /
PubMed AbstractN-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction is catalysed by an eight-protein ...N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction is catalysed by an eight-protein oligosaccharyltransferase (OST) complex that is embedded in the endoplasmic reticulum membrane. Our understanding of eukaryotic protein N-glycosylation has been limited owing to the lack of high-resolution structures. Here we report a 3.5 Å resolution cryo-electron microscopy structure of the Saccharomyces cerevisiae OST complex, revealing the structures of subunits Ost1-Ost5, Stt3, Wbp1 and Swp1. We found that seven phospholipids mediate many of the inter-subunit interactions, and an Stt3 N-glycan mediates interactions with Wbp1 and Swp1 in the lumen. Ost3 was found to mediate the OST-Sec61 translocon interface, funnelling the acceptor peptide towards the OST catalytic site as the nascent peptide emerges from the translocon. The structure provides insights into co-translational protein N-glycosylation, and may facilitate the development of small-molecule inhibitors that target this process.
External linksNature / PubMed:29466327 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

7336

6c26

EMDB-7336, PDB-6c26:
The Cryo-EM structure of a eukaryotic oligosaccharyl transferase complex
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-EGY:
(4R,7R)-4-hydroxy-N,N,N-trimethyl-4,9-dioxo-7-[(undecanoyloxy)methyl]-3,5,8-trioxa-4lambda~5~-phosphadocosan-1-aminium / phospholipid*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • Baker's yeast (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsTRANSFERASE / complex / glycosylation

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