Cryo–electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B | Zendy

Ana S. Ramírez | Zendy; Julia Kowal | Zendy; Kaspar P. Locher | Zendy

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Cryo–electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B

Author(s) -

Ana S. Ramírez,

Julia Kowal,

Kaspar P. Locher

Publication year - 2019

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aaz3505

Subject(s) - endoplasmic reticulum , glycan , ribosome , chemistry , affinities , cryo electron microscopy , biology , peptide , microbiology and biotechnology , biophysics , biochemistry , glycoprotein , gene , rna

A division of labor for glycosylation Glycosylation is a ubiquitous modification of eukaryotic secreted proteins. Asparagine-linked chains of sugars are appended to many substrates as they are translocated into the endoplasmic reticulum. Ramírezet al. solved cryo–electron microscopy structures of two human oligosaccharyltransferase complexes, OST-A and OST-B. The catalytic subunits bind partner proteins that direct glycosylation of specific substrates either cotranslationally (OST-A) or on fully folded proteins (OST-B). High-resolution views of the active site and bound substrates in one of the complexes reveal important features of the human enzymes.Science , this issue p.1372

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