Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation-Reference-Cited by-同舟云学术

Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation

Published:2018-02-02 Issue:6375 Volume:359 Page:545-550
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Wild Rebekka¹^ORCID,Kowal Julia¹^ORCID,Eyring Jillianne²^ORCID,Ngwa Elsy M.²^ORCID,Aebi Markus²^ORCID,Locher Kaspar P.¹^ORCID

Affiliation:

1. Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, CH-8093 Zurich, Switzerland.

2. Institute of Microbiology, Department of Biology, ETH Zurich, CH-8093 Zurich, Switzerland.

Abstract

Remember the sugar when making proteins Eukaryotes have an elaborate trafficking and quality-control system for secreted glycoproteins. The glycosylation pathway begins in the endoplasmic reticulum with the enzyme oligosaccharyltransferase (OST), which attaches a long chain of sugars to asparagine residues of target proteins. Wild et al. report a cryo-electron microscopy structure of yeast OST, which includes eight separate membrane proteins. The central catalytic subunit contains binding sites for substrates and is flanked by accessory subunits that may facilitate delivery of newly translocated proteins for glycosylation. Science , this issue p. 545

Funder

Swiss National Science Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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