7CK2

Crystal structure of Arabidopsis CESA3 catalytic domain with UDP-Glucose

Summary for 7CK2

• Entry DOI: 10.2210/pdb7ck2/pdb
• Descriptor: Cellulose synthase A catalytic subunit 3 [UDP-forming],Cellulose synthase A catalytic subunit 3 [UDP-forming], MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE-GLUCOSE, ... (4 entities in total)
• Functional Keywords: enzyme, synthase, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 2
• Total formula weight: 93294.90

Authors

Qiao, Z.,Gao, Y.G. (deposition date: 2020-07-15, release date: 2021-03-17, Last modification date: 2024-10-23)

Primary citation

Qiao, Z.,Lampugnani, E.R.,Yan, X.F.,Khan, G.A.,Saw, W.G.,Hannah, P.,Qian, F.,Calabria, J.,Miao, Y.,Gruber, G.,Persson, S.,Gao, Y.G.
Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed 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 CESA3 (AtCESA3) in both apo and uridine diphosphate (UDP)-glucose (UDP-Glc)-bound forms. AtCESA3 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 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 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 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.

PubMed: 33729990
DOI: 10.1073/pnas.2024015118

Experimental method

X-RAY DIFFRACTION (2.05 Å)