Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis. / 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.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 118, No. 11, e2024015118, 2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Qiao, Z, Lampugnani, ER, Yan, XF, Khan, GA, Saw, WG, Hannah, P, Qian, F, Calabria, J, Miao, Y, Grüber, G, Persson, S & Gao, Y-G 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, vol. 118, no. 11, e2024015118. https://doi.org/10.1073/pnas.2024015118

APA

Qiao, Z., Lampugnani, E. R., Yan, X. F., Khan, G. A., Saw, W. G., Hannah, P., Qian, F., Calabria, J., Miao, Y., Grüber, G., Persson, S., & Gao, Y-G. (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://doi.org/10.1073/pnas.2024015118

Vancouver

Qiao Z, Lampugnani ER, Yan XF, Khan GA, Saw WG, Hannah P et al. 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. 2021;118(11). e2024015118. https://doi.org/10.1073/pnas.2024015118

Author

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. / Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis. In: Proceedings of the National Academy of Sciences of the United States of America. 2021 ; Vol. 118, No. 11.

Bibtex

@article{3b8326da6d314d7093fd5cea27edddea,
title = "Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis",
abstract = "Cellulose is synthesized by cellulose synthases (CESAs) from the glycosyltransferase GT-2 family. In plants, the CESAs form a sixlobed 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. AtCESA3CatDhas 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 AtCESA3CatDonto 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 AtCESA3CatDcan 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 CESAsmight dimerize to eventually assemble into CSCs in plants.",
keywords = "Cellulose synthase, Plant biology, Plant cell wall, Structural biology, UDP-glucose",
author = "Zhu Qiao and Lampugnani, {Edwin R.} and Yan, {Xin Fu} and Khan, {Ghazanfar Abbas} and Saw, {Wuan Geok} and Patrick Hannah and Feng Qian and Jacob Calabria and Yansong Miao and Gerhard Gr{\"u}ber and Staffan Persson and Yong-Gui Gao",
year = "2021",
doi = "10.1073/pnas.2024015118",
language = "English",
volume = "118",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "11",

}

RIS

TY - JOUR

T1 - Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis

AU - Qiao, Zhu

AU - Lampugnani, Edwin R.

AU - Yan, Xin Fu

AU - Khan, Ghazanfar Abbas

AU - Saw, Wuan Geok

AU - Hannah, Patrick

AU - Qian, Feng

AU - Calabria, Jacob

AU - Miao, Yansong

AU - Grüber, Gerhard

AU - Persson, Staffan

AU - Gao, Yong-Gui

PY - 2021

Y1 - 2021

N2 - Cellulose is synthesized by cellulose synthases (CESAs) from the glycosyltransferase GT-2 family. In plants, the CESAs form a sixlobed 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. AtCESA3CatDhas 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 AtCESA3CatDonto 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 AtCESA3CatDcan 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 CESAsmight dimerize to eventually assemble into CSCs in plants.

AB - Cellulose is synthesized by cellulose synthases (CESAs) from the glycosyltransferase GT-2 family. In plants, the CESAs form a sixlobed 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. AtCESA3CatDhas 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 AtCESA3CatDonto 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 AtCESA3CatDcan 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 CESAsmight dimerize to eventually assemble into CSCs in plants.

KW - Cellulose synthase

KW - Plant biology

KW - Plant cell wall

KW - Structural biology

KW - UDP-glucose

U2 - 10.1073/pnas.2024015118

DO - 10.1073/pnas.2024015118

M3 - Journal article

C2 - 33729990

AN - SCOPUS:85102377529

VL - 118

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 11

M1 - e2024015118

ER -

ID: 259678421