Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis
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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.
Originalsprog | Engelsk |
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Artikelnummer | e2024015118 |
Tidsskrift | Proceedings of the National Academy of Sciences of the United States of America |
Vol/bind | 118 |
Udgave nummer | 11 |
ISSN | 0027-8424 |
DOI | |
Status | Udgivet - 2021 |
Links
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7980446/pdf/pnas.202024015.pdf
Forlagets udgivne version
ID: 259678421