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-Structure paper
タイトル | The atomic structure of a eukaryotic oligosaccharyltransferase complex. |
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ジャーナル・号・ページ | Nature, Vol. 555, Issue 7696, Page 328-333, Year 2018 |
掲載日 | 2018年3月15日 |
著者 | Lin Bai / Tong Wang / Gongpu Zhao / Amanda Kovach / Huilin Li / |
PubMed 要旨 | 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 ...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. |
リンク | Nature / PubMed:29466327 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.5 Å |
構造データ | |
化合物 | ChemComp-EGY: ChemComp-NAG: |
由来 |
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キーワード | TRANSFERASE / complex / glycosylation |