8VHZ

Cryo EM structure of a soybean CesA1 homotrimer

Summary for 8VHZ

• Entry DOI: 10.2210/pdb8vhz/pdb
• EMDB information: 43244
• Descriptor: Cellulose synthase (1 entity in total)
• Functional Keywords: cellulose, glycosyltransferase, microfibril, transferase
• Biological source: Glycine max (soybean)
• Total number of polymer chains: 3
• Total formula weight: 366745.57

Authors

Ho, R.,Palliniti, P.,Zimmer, J. (deposition date: 2024-01-02, release date: 2025-01-15, Last modification date: 2025-06-04)

Primary citation

Ho, R.,Pallinti, P.,Wilson, L.F.L.,Wan, Y.,Zimmer, J.
Structure, function and assembly of soybean primary cell wall cellulose synthases.
Elife, 13:-, 2025

PubMed Abstract: Plant cell walls contain a meshwork of cellulose fibers embedded into a matrix of other carbohydrate and non-carbohydrate-based biopolymers. This composite material exhibits extraordinary properties, from stretchable and pliable cell boundaries to solid protective shells. Cellulose, a linear glucose polymer, is synthesized and secreted across the plasma membrane by cellulose synthase (CesA), of which plants express multiple isoforms. Different subsets of CesA isoforms are necessary for primary and secondary cell wall biogenesis. Here, we structurally and functionally characterize the (soybean) primary cell wall CesAs CesA1, CesA3, and CesA6. The CesA isoforms exhibit robust in vitro catalytic activity. Cryo-electron microscopy analyses reveal their assembly into homotrimeric complexes in vitro in which each CesA protomer forms a cellulose-conducting transmembrane channel with a large lateral opening. Biochemical and co-purification analyses demonstrate that different CesA isoforms interact in vitro, leading to synergistic cellulose biosynthesis. Interactions between CesA trimers are only observed between different CesA isoforms and require the class-specific region (CSR). The CSR forms a hook-shaped extension of CesA's catalytic domain at the cytosolic water-lipid interface. Negative stain and cryo-electron microscopy analyses of mixtures of different CesA isoform trimers reveal their side-by-side arrangement into loose clusters. Our data suggest a model by which CesA homotrimers of different isoforms assemble into cellulose synthase complexes to synthesize and secrete multiple cellulose chains for microfibril formation. Inter-trimer interactions are mediated by fuzzy interactions between their CSR extensions.

PubMed: 40365874
DOI: 10.7554/eLife.96704

Experimental method

ELECTRON MICROSCOPY (3.3 Å)