Mechanism of Glycosylation

  • Author: ChemistryViews
  • Published: 04 July 2011
  • Copyright: Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
  • Source / Publisher: Nature/Nature Publishing Group
thumbnail image: Mechanism of Glycosylation

The process of N-linked glycosylation is essential for cells of higher organisms. It plays a role in a multitude of cellular functions and is performed by the membrane protein complex oligosaccharyltransferase (OST). OST catalyzes the glycosylation of asparagines via a nitrogen group, but the mechanism is unknown.

Kaspar Locher and co-workers, ETH Zürich, Switzerland, have determined the structure of OST to help understand how it operates. The team isolated and crystallized OST from the bacteria Campylobacter lari and studied it with X-ray crystallography. They see a novel fold in the transmembrane domain wherein 13 transmembrane segments are connected by external loops. One of these loops, EL5, is predicted to play an important role in OST's activity: EL5 is expected to become ordered upon peptide binding and pins the peptide in place. This forms the catalytic site. This would enable a mechanism whereby binding of a lipid-linked oligosaccharide would result in a nucleophilic attack of the activated amide nitrogen, leading to glycosylation.

Article Views: 3225

Sign in Area

Please sign in below

Additional Sign In options

Please note that to comment on an article you must be registered and logged in.
Registration is for free, you may already be registered to receive, e.g., the newsletter. When you register on this website, please ensure you view our terms and conditions. All comments are subject to moderation.

Article Comments - To add a comment please sign in

If you would like to reuse any content, in print or online, from, please contact us first for permission. more

Follow on Facebook Follow on Twitter Follow on LinkedIn Follow on Instagram RSS Sign up for newsletters

Magazine of Chemistry Europe (16 European Chemical Societies) published by Wiley-VCH