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The Atomic Structure of a Eukaryotic Oligosaccharyltransferase Complex

The Atomic Structure of a Eukaryotic Oligosaccharyltransferase Complex

Lin Bai, Tong Wang, Gongpu Zhao, Amanda Kovach, Huilin Li

Nature. 2018 Mar 15;555(7696):328-333.

PMID: 29466327

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP145164245	A3 Glycan		145164-24-5	Price

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