Journal article

Differences in protein structural regions that impact functional specificity in GT2 family beta-glucan synthases

Daniel P Oehme, Thomas Shafee, Matthew T Downton, Antony Bacic, Monika S Doblin

PLoS One | PUBLIC LIBRARY SCIENCE | Published : 2019

Abstract

Most cell wall and secreted β-glucans are synthesised by the CAZy Glycosyltransferase 2 family (www.cazy.org), with different members catalysing the formation of (1,4)-β-, (1,3)-β-, or both (1,4)- and (1,3)-β-glucosidic linkages. Given the distinct physicochemical properties of each of the resultant β-glucans (cellulose, curdlan, and mixed linkage glucan, respectively) are crucial to their biological and biotechnological functions, there is a desire to understand the molecular evolution of synthesis and how linkage specificity is determined. With structural studies hamstrung by the instability of these proteins to solubilisation, we have utilised in silico techniques and the crystal structur..

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Grants

Awarded by Australia Research Council


Awarded by Victorian Life Sciences Computation Initiative (VLSCI)


Funding Acknowledgements

This work was funded by a grant from the Australia Research Council to the ARC Centre of Excellence in Plant Cell Walls (to DPO, MSD and AB) (CE110001007); and the Victorian Life Sciences Computation Initiative (VLSCI) grant numbers "VR0319'' on its Peak Computing Facility at the University of Melbourne, an initiative of the Victorian State Government (to DPO). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.