Issue 12, 2015

Molecular-scale features that govern the effects of O-glycosylation on a carbohydrate-binding module

Abstract

Protein glycosylation is a ubiquitous post-translational modification in all kingdoms of life. Despite its importance in molecular and cellular biology, the molecular-level ramifications of O-glycosylation on biomolecular structure and function remain elusive. Here, we took a small model glycoprotein and changed the glycan structure and size, amino acid residues near the glycosylation site, and glycosidic linkage while monitoring any corresponding changes to physical stability and cellulose binding affinity. The results of this study reveal the collective importance of all the studied features in controlling the most pronounced effects of O-glycosylation in this system. Going forward, this study suggests the possibility of designing proteins with multiple improved properties by simultaneously varying the structures of O-glycans and amino acids local to the glycosylation site.

Graphical abstract: Molecular-scale features that govern the effects of O-glycosylation on a carbohydrate-binding module

Supplementary files

Article information

Article type
Edge Article
Submitted
21 Jul 2015
Accepted
16 Sep 2015
First published
21 Sep 2015
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2015,6, 7185-7189

Molecular-scale features that govern the effects of O-glycosylation on a carbohydrate-binding module

X. Guan, P. K. Chaffey, C. Zeng, E. R. Greene, L. Chen, M. R. Drake, C. Chen, A. Groobman, M. G. Resch, M. E. Himmel, G. T. Beckham and Z. Tan, Chem. Sci., 2015, 6, 7185 DOI: 10.1039/C5SC02636A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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