6WLB
Structure of homotrimeric poplar cellulose synthase isoform 8
Summary for 6WLB
Entry DOI | 10.2210/pdb6wlb/pdb |
EMDB information | 21820 |
Related PRD ID | PRD_900016 |
Descriptor | Cellulose synthase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose (2 entities in total) |
Functional Keywords | cellulose, polysaccharide, cell wall, glycosyltransferase, membrane protein, translocation |
Biological source | Populus tremula x Populus tremuloides (Hybrid aspen) |
Total number of polymer chains | 3 |
Total formula weight | 339935.23 |
Authors | Zimmer, J.,Pallinti, P.,Ho, R. (deposition date: 2020-04-19, release date: 2020-07-22, Last modification date: 2024-03-06) |
Primary citation | Purushotham, P.,Ho, R.,Zimmer, J. Architecture of a catalytically active homotrimeric plant cellulose synthase complex. Science, 369:1089-1094, 2020 Cited by PubMed Abstract: Cellulose is an essential plant cell wall component and represents the most abundant biopolymer on Earth. Supramolecular plant cellulose synthase complexes organize multiple linear glucose polymers into microfibrils as load-bearing wall components. We determined the structure of a poplar cellulose synthase CesA homotrimer that suggests a molecular basis for cellulose microfibril formation. This complex, stabilized by cytosolic plant-conserved regions and helical exchange within the transmembrane segments, forms three channels occupied by nascent cellulose polymers. Secretion steers the polymers toward a common exit point, which could facilitate protofibril formation. CesA's N-terminal domains assemble into a cytosolic stalk that interacts with a microtubule-tethering protein and may thus be involved in CesA localization. Our data suggest how cellulose synthase complexes assemble and provide the molecular basis for plant cell wall engineering. PubMed: 32646917DOI: 10.1126/science.abb2978 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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