The atomic structure of a eukaryotic oligosaccharyltransferase complex

Lin Bai, Tong Wang, Gongpu Zhao, Amanda Kovach and Huilin Li ()
Additional contact information
Lin Bai: Center for Epigenetics, Van Andel Research Institute
Tong Wang: Advanced Science Research Center at the Graduate Center of the City University of New York
Gongpu Zhao: David Van Andel Advanced Cryo-Electron Microscopy Suite, Van Andel Research Institute
Amanda Kovach: Center for Epigenetics, Van Andel Research Institute
Huilin Li: Center for Epigenetics, Van Andel Research Institute

Nature, 2018, vol. 555, issue 7696, 328-333

Abstract: Abstract 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.

Date: 2018
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature25755 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:555:y:2018:i:7696:d:10.1038_nature25755

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature25755

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().