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TitleArchitecture of a catalytically active homotrimeric plant cellulose synthase complex.
Journal, issue, pagesScience, Vol. 369, Issue 6507, Page 1089-1094, Year 2020
Publish dateAug 28, 2020
AuthorsPallinti Purushotham / Ruoya Ho / Jochen Zimmer /
PubMed AbstractCellulose 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 ...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.
External linksScience / PubMed:32646917
MethodsEM (single particle)
Resolution3.5 Å
Structure data

21820

6wlb

EMDB-21820, PDB-6wlb:
Structure of homotrimeric poplar cellulose synthase isoform 8
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • populus tremula x populus tremuloides (plant)
KeywordsMEMBRANE PROTEIN / Cellulose / polysaccharide / cell wall / glycosyltransferase / translocation

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