Research Article

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

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Science  02 Feb 2018:
Vol. 359, Issue 6375, pp. 545-550
DOI: 10.1126/science.aar5140

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


Oligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate–activated donor to glycosylation sites of secretory proteins. Here we describe the atomic structure of yeast OST determined by cryo–electron microscopy, revealing a conserved subunit arrangement. The active site of the catalytic STT3 subunit points away from the center of the complex, allowing unhindered access to substrates. The dolichol-pyrophosphate moiety binds to a lipid-exposed groove of STT3, whereas two noncatalytic subunits and an ordered N-glycan form a membrane-proximal pocket for the oligosaccharide. The acceptor polypeptide site faces an oxidoreductase domain in stand-alone OST complexes or is immediately adjacent to the translocon, suggesting how eukaryotic OSTs efficiently glycosylate a large number of polypeptides before their folding.

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