| Literature DB >> 30450807 |
Abstract
N-glycosylation is one of the predominant modifications of eukaryotic proteins. It is catalyzed by oligosaccharyl transferase (OST), an eight-subunit protein complex in the endoplasmic reticulum membrane. OST transfers the oligosaccharide from a lipid-linked donor (LLO) to the Asn-Xaa-Ser/Thr sequon of nascent polypeptide, usually cotranslationally by partnering with the ribosome and the translocon. We and two other groups have recently determined high-resolution cryo-EM structures of the yeast and mammalian OST complexes. In this Structural Snapshot, we describe the molecular mechanism of eukaryotic OST and its interaction with the translocon.Entities:
Keywords: zzm321990Saccharomyces cerevisiaezzm321990; cryo-EM; glycosyltransferase; protein N-glycosylation; protein structure; structural biology
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Year: 2018 PMID: 30450807 PMCID: PMC6504584 DOI: 10.1111/febs.14705
Source DB: PubMed Journal: FEBS J ISSN: 1742-464X Impact factor: 5.542