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Cryo‐ EM is uncovering the mechanism of eukaryotic protein N‐glycosylation
Author(s) -
Bai Lin,
Li Huilin
Publication year - 2019
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14705
Subject(s) - translocon , endoplasmic reticulum , glycosylation , chemistry , protein subunit , microbiology and biotechnology , ribosome , n linked glycosylation , biochemistry , membrane protein , biology , glycoprotein , membrane , rna , gene , glycan
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.