Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis
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 dip...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Journal Article |
| Language: | English |
| Published: |
2021
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| Online Access: | https://hdl.handle.net/10356/148273 |
| _version_ | 1826114665251340288 |
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| 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 |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences 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 |
| author_sort | Qiao, Zhu |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T03:42:50Z |
| format | Journal Article |
| id | ntu-10356/148273 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T03:42:50Z |
| publishDate | 2021 |
| record_format | dspace |
| spelling | ntu-10356/1482732023-02-28T17:09:17Z 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 School of Biological Sciences NTU Institute of Structural Biology Science::Biological sciences Cellulose Synthase Structural Biology 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. Ministry of Education (MOE) Accepted version This work was supported by a Tier II grant MOE2019-T2-2-099 from the Ministry of Education (MOE) of Singapore (Y.-G.G.), and ARC FT and DP grants (DP190101941; FT160100218), Villum Investigator (Project ID: 25915) and Novo Nordisk Laureate (NNF19OC0056076) grants (SP). 2021-05-05T02:31:20Z 2021-05-05T02:31:20Z 2021 Journal Article 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 11 https://hdl.handle.net/10356/148273 10.1073/pnas.2024015118 33729990 2-s2.0-85102377529 11 118 e2024015118 en Proceedings of the National Academy of Sciences of the United States of America © 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). application/pdf |
| spellingShingle | Science::Biological sciences Cellulose Synthase Structural Biology 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 |
| title | Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis |
| title_full | Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis |
| title_fullStr | Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis |
| title_full_unstemmed | Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis |
| title_short | Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis |
| title_sort | structure of arabidopsis cesa3 catalytic domain with its substrate udp glucose provides insight into the mechanism of cellulose synthesis |
| topic | Science::Biological sciences Cellulose Synthase Structural Biology |
| url | https://hdl.handle.net/10356/148273 |
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