Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/148273
Title: Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis
Authors: Qiao, Zhu
Lampugnani, Edwin R.
Yan, Xin-Fu
Khan, Ghazanfar Abbas
Saw, Wuan Geok
Hannah, Patrick
Qian, Feng
Calabria, Jacob
Miao, Yansong
Grüber, Gerhard
Persson, Staffan
Gao, Yong-Gui
Keywords: Science::Biological sciences
Issue Date: 2021
Source: Qiao, Z., Lampugnani, E. R., Yan, X., Khan, G. A., Saw, W. G., Hannah, P., Qian, F., Calabria, J., Miao, Y., Grüber, G., Persson, S. & Gao, Y. (2021). Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis. Proceedings of the National Academy of Sciences of the United States of America, 118(11), e2024015118-. https://dx.doi.org/10.1073/pnas.2024015118
Journal: Proceedings of the National Academy of Sciences of the United States of America
Abstract: Cellulose is synthesized by cellulose synthases (CESAs) from the glycosyltransferase GT-2 family. In plants, the CESAs form a six-lobed rosette-shaped CESA complex (CSC). Here we report crystal structures of the catalytic domain of Arabidopsis thaliana CESA3 (AtCESA3CatD) in both apo and uridine diphosphate (UDP)-glucose (UDP-Glc)–bound forms. AtCESA3CatD has an overall GT-A fold core domain sandwiched between a plant-conserved region (P-CR) and a class-specific region (C-SR). By superimposing the structure of AtCESA3CatD onto the bacterial cellulose synthase BcsA, we found that the coordination of the UDP-Glc differs, indicating different substrate coordination during cellulose synthesis in plants and bacteria. Moreover, structural analyses revealed that AtCESA3CatD can form a homodimer mainly via interactions between specific beta strands. We confirmed the importance of specific amino acids on these strands for homodimerization through yeast and in planta assays using point-mutated full-length AtCESA3. Our work provides molecular insights into how the substrate UDP-Glc is coordinated in the CESAs and how the CESAs might dimerize to eventually assemble into CSCs in plants.
URI: https://hdl.handle.net/10356/148273
ISSN: 11
DOI: 10.1073/pnas.2024015118
Rights: © 2021 The Author(s) (Published by National Academy of Sciences). All rights reserved. This paper was published in Proceedings of the National Academy of Sciences of the United States of America and is made available with permission of The Author(s) (Published by National Academy of Sciences).
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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