7ck3
From Proteopedia
Crystal structure of Arabidopsis CESA3 catalytic domain
Structural highlights
FunctionCESA3_ARATH Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation, especially in roots.[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedCellulose 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 (AtCESA3(CatD)) in both apo and uridine diphosphate (UDP)-glucose (UDP-Glc)-bound forms. AtCESA3(CatD) 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 AtCESA3(CatD) 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 AtCESA3(CatD) 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. Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis.,Qiao Z, Lampugnani ER, Yan XF, Khan GA, Saw WG, Hannah P, Qian F, Calabria J, Miao Y, Gruber G, Persson S, Gao YG Proc Natl Acad Sci U S A. 2021 Mar 16;118(11). pii: 2024015118. doi:, 10.1073/pnas.2024015118. PMID:33729990[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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