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Title: Molecular-Scale Features that Govern the Effects of O-Glycosylation on a Carbohydrate-Binding Module

Journal Article · · Chemical Science
DOI:https://doi.org/10.1039/C5SC02636A· OSTI ID:1233680

The 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. 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.

Research Organization:
National Renewable Energy Laboratory (NREL), Golden, CO (United States)
Sponsoring Organization:
USDOE Office of Energy Efficiency and Renewable Energy (EERE), Sustainable Transportation Office. Bioenergy Technologies Office (BETO)
Grant/Contract Number:
AC36-08GO28308
OSTI ID:
1233680
Report Number(s):
NREL/JA-5100-65609
Journal Information:
Chemical Science, Vol. 6, Issue 12; Related Information: Chemical Science; ISSN 2041-6520
Publisher:
Royal Society of ChemistryCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 26 works
Citation information provided by
Web of Science

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Cited By (6)

Just a spoonful of sugar: Short glycans affect protein properties and functions journal March 2019
Engineering enhanced cellobiohydrolase activity journal March 2018
Role of glycosylation in nucleating protein folding and stability journal July 2017
Distinct roles of N- and O-glycans in cellulase activity and stability journal December 2017
The influence of different linker modifications on the catalytic activity and cellulose affinity of cellobiohydrolase Cel7A from Hypocrea jecorina journal July 2017
A novel, highly efficient β-glucosidase with a cellulose-binding domain: characterization and properties of native and recombinant proteins journal November 2017

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