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Issue 34, 2020
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Carbohydrate-binding module O-mannosylation alters binding selectivity to cellulose and lignin

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Abstract

Improved understanding of the effect of protein glycosylation is expected to provide the foundation for the design of protein glycoengineering strategies. In this study, we examine the impact of O-glycosylation on the binding selectivity of a model Family 1 carbohydrate-binding module (CBM), which has been shown to be one of the primary sub-domains responsible for non-productive lignin binding in multi-modular cellulases. Specifically, we examine the relationship between glycan structure and the binding specificity of the CBM to cellulose and lignin substrates. We find that the glycosylation pattern of the CBM exhibits a strong influence on the binding affinity and the selectivity between both cellulose and lignin. In addition, the large set of binding data collected allows us to examine the relationship between binding affinity and the correlation in motion between pairs of glycosylation sites. Our results suggest that glycoforms displaying highly correlated motion in their glycosylation sites tend to bind cellulose with high affinity and lignin with low affinity. Taken together, this work helps lay the groundwork for future exploitation of glycoengineering as a tool to improve the performance of industrial enzymes.

Graphical abstract: Carbohydrate-binding module O-mannosylation alters binding selectivity to cellulose and lignin

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Supplementary files

Article information


Submitted
29 Mar 2020
Accepted
16 Aug 2020
First published
19 Aug 2020

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2020,11, 9262-9271
Article type
Edge Article

Carbohydrate-binding module O-mannosylation alters binding selectivity to cellulose and lignin

Y. Li, X. Guan, P. K. Chaffey, Y. Ruan, B. Ma, S. Shang, M. E. Himmel, G. T. Beckham, H. Long and Z. Tan, Chem. Sci., 2020, 11, 9262
DOI: 10.1039/D0SC01812K

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