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Title: Insights into substrate coordination and glycosyl transfer of poplar cellulose synthase-8

Journal Article · · Structure
 [1];  [2];  [3];  [2]; ORCiD logo [3]
  1. University of Virginia, Charlottesville, VA (United States); Howard Hughes Medical Institute / University of Virginia
  2. North Carolina State University, Raleigh, NC (United States)
  3. University of Virginia, Charlottesville, VA (United States)

Cellulose is an abundant cell wall component of land plants. It is synthesized from UDP-activated glucose molecules by cellulose synthase, a membrane-integrated processive glycosyltransferase. Cellulose synthase couples the elongation of the cellulose polymer with its translocation across the plasma membrane. Here, we present substrate- and product-bound cryogenic electron microscopy structures of the homotrimeric cellulose synthase isoform-8 (CesA8) from hybrid aspen (poplar). UDP-glucose binds to a conserved catalytic pocket adjacent to the entrance to a transmembrane channel. The substrate’s glucosyl unit is coordinated by conserved residues of the glycosyltransferase domain and amphipathic interface helices. Site-directed mutagenesis of a conserved gating loop capping the active site reveals its critical function for catalytic activity. Molecular dynamics simulations reveal prolonged interactions of the gating loop with the substrate molecule, particularly across its central conserved region. These transient interactions likely facilitate the proper positioning of the substrate molecule for glycosyl transfer and cellulose translocation.

Research Organization:
Center for Lignocellulose Structure and Formation, Raleigh, NC (United States)
Sponsoring Organization:
National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
SC0001090
OSTI ID:
2208811
Journal Information:
Structure, Journal Name: Structure Journal Issue: 10 Vol. 31; ISSN 0969-2126
Publisher:
ElsevierCopyright Statement
Country of Publication:
United States
Language:
English

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