6c26

Publication Abstract from PubMed

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 complex, OST, embedded in the ER 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-A resolution cryo-EM structure of the Saccharomyces cerevisiae OST, revealing the structures of Ost1-5, 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 novel insights into co-translational protein N-glycosylation and may facilitate the development of small-molecule inhibitors targeting this process.

The atomic structure of a eukaryotic oligosaccharyltransferase complex.,Bai L, Wang T, Zhao G, Kovach A, Li H Nature. 2018 Jan 22. pii: nature25755. doi: 10.1038/nature25755. PMID:29466327^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.