Structure of <i>Arabidopsis</i> CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis
Qiao Zhu, Edwin R. Lampugnani, Xin‐Fu Yan, Ghazanfar Abbas Khan, Wuan Geok Saw, Patrick Hannah, Feng Qian, Jacob Calabria, Yansong Miao, Gerhard Grüber, Staffan Persson, Yong‐Gui Gao
Abstract
Significance Cellulose is the most abundant biopolymer on Earth and has many potential industrial applications, such as renewable energy and sustainable materials. Here we report the apo and UDP-glucose (UDP-Glc)–bound crystal structures of the catalytic domain of Arabidopsis thaliana CESA3. Our results offer a structural basis for how the substrate UDP-Glc and a metal ion, Mn 2+ , which is required for cellulose synthesis, are coordinated in plant CESAs. Furthermore, our structure reveals that CESAs may form homodimers through interactions between specific beta strands that likely aid in the early stages of CESA complex formation.