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https://hdl.handle.net/2440/139288
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Type: | Journal article |
Title: | Enzymes in 3D: Synthesis, remodelling, and hydrolysis of cell wall (1,3;1,4)-β-glucans |
Other Titles: | Enzymes in 3D: Synthesis, remodelling, and hydrolysis of cell wall (1,3;1,4)-beta-glucans |
Author: | Hrmova, M. Zimmer, J. Bulone, V. Fincher, G.B. |
Citation: | Plant Physiology, 2024; 194(1):33-50 |
Publisher: | American Society of Plant Biologists |
Issue Date: | 2024 |
ISSN: | 0032-0889 1532-2548 |
Statement of Responsibility: | Maria Hrmova, Jochen Zimmer, Vincent Bulone and Geoffrey B. Fincher |
Abstract: | Recent breakthroughs in structural biology have provided valuable new insights into enzymes involved in plant cell wall metabolism. More specifically, the molecular mechanism of synthesis of (1,3;1,4)-β-glucans, which are widespread in cell walls of commercially important cereals and grasses, has been the topic of debate and intense research activity for decades. However, an inability to purify these integral membrane enzymes or apply transgenic approaches without interpretative problems associated with pleiotropic effects has presented barriers to attempts to define their synthetic mechanisms. Following the demonstration that some members of the CslF sub-family of GT2 family enzymes mediate (1,3;1,4)-β-glucan synthesis, the expression of the corresponding genes in a heterologous system that is free of background complications has now been achieved. Biochemical analyses of the (1,3;1,4)-β-glucan synthesized in vitro, combined with 3-dimensional (3D) cryogenic-electron microscopy and AlphaFold protein structure predictions, have demonstrated how a single CslF6 enzyme, without exogenous primers, can incorporate both (1,3)- and (1,4)-β-linkages into the nascent polysaccharide chain. Similarly, 3D structures of xyloglucan endo-transglycosylases and (1,3;1,4)-β-glucan endo- and exohydrolases have allowed the mechanisms of (1,3;1,4)-β-glucan modification and degradation to be defined. X-ray crystallography and multi-scale modeling of a broad specificity GH3 β-glucan exohydrolase recently revealed a previously unknown and remarkable molecular mechanism with reactant trajectories through which a polysaccharide exohydrolase can act with a processive action pattern. The availability of high-quality protein 3D structural predictions should prove invaluable for defining structures, dynamics, and functions of other enzymes involved in plant cell wall metabolism in the immediate future. |
Keywords: | Cell Wall Poaceae Polysaccharides beta-Glucans Hydrolysis |
Description: | Advance access publication August 18, 2023 |
Rights: | © The Author(s) 2023. Published by Oxford University Press on behalf of American Society of Plant Biologists. This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits noncommercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
DOI: | 10.1093/plphys/kiad415 |
Grant ID: | http://purl.org/au-research/grants/arc/CE1101007 http://purl.org/au-research/grants/arc/DP180103974 http://purl.org/au-research/grants/arc/DP120100900 |
Published version: | http://dx.doi.org/10.1093/plphys/kiad415 |
Appears in Collections: | Agriculture, Food and Wine publications |
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File | Description | Size | Format | |
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hdl_139288.pdf | Published version | 8.71 MB | Adobe PDF | View/Open |
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