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Architecture of a catalytically active homotrimeric plant cellulose synthase complex

Journal Article · · Science
 [1];  [2];  [2]
  1. Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, 480 Ray C. Hunt Dr., Charlottesville, VA 22903, USA.; OSTI
  2. Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, 480 Ray C. Hunt Dr., Charlottesville, VA 22903, USA.

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.

Research Organization:
Pennsylvania State Univ., University Park, PA (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
DOE Contract Number:
SC0001090
OSTI ID:
1801446
Journal Information:
Science, Journal Name: Science Journal Issue: 6507 Vol. 369; ISSN 0036-8075
Publisher:
AAAS
Country of Publication:
United States
Language:
English

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