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DOI	10.1073/pnas.2024015118
	Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis
	Qiao Z.; Lampugnani E.R.; Yan X.-F.; Khan G.A.; Saw W.G.; Hannah P.; Qian F.; Calabria J.; Miao Y.; Grüber G.; Persson S.; Gao Y.-G.
发表日期	2021
ISSN	00278424
卷号	118 期号:11
英文摘要	Cellulose is synthesized by cellulose synthases (CESAs) from the glycosyltransferase GT-2 family. In plants, the CESAs form a sixlobed rosette-shaped CESA complex (CSC). Here we report crystal structures of the catalytic domain of Arabidopsis thaliana CESA3 (AtCESA3CatD) in both apo and uridine diphosphate (UDP)-glucose (UDP-Glc)-bound forms. AtCESA3CatDhas an overall GT-A fold core domain sandwiched between a plant-conserved region (P-CR) and a class-specific region (C-SR). By superimposing the structure of AtCESA3CatDonto the bacterial cellulose synthase BcsA, we found that the coordination of the UDP-Glc differs, indicating different substrate coordination during cellulose synthesis in plants and bacteria. Moreover, structural analyses revealed that AtCESA3CatDcan form a homodimer mainly via interactions between specific beta strands. We confirmed the importance of specific amino acids on these strands for homodimerization through yeast and in planta assays using point-mutated full-length AtCESA3. Our work provides molecular insights into how the substrate UDP-Glc is coordinated in the CESAs and how the CESAsmight dimerize to eventually assemble into CSCs in plants. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Cellulose synthase; Plant biology; Plant cell wall; Structural biology; UDP-glucose
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180236
作者单位	School of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore; NTU Institute of Structural Biology, Nanyang Technological University, Singapore, 639798, Singapore; School of Biosciences, University of Melbourne, Parkville, VIC 3010, Australia; Department of Animal, Plant and Soil Sciences, School of Life Sciences, La Trobe University, Bundoora, VIC 3086, Australia; Division of Molecular Biology, Shanghai Genomics, Inc., Shanghai, 201202, China; Department of Plant and Environmental Sciences, University of Copenhagen, Frederiksberg C, 1871, Denmark; Joint International Research Laboratory of Metabolic & Developmental Sciences, State Key Laboratory of Hybrid Rice, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, China; Copenhagen Plant Science Center, University of Copenhagen, Frederiksberg C, 1871, Denmark
推荐引用方式 GB/T 7714	Qiao Z.,Lampugnani E.R.,Yan X.-F.,et al. Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis[J],2021,118(11).
APA	Qiao Z..,Lampugnani E.R..,Yan X.-F..,Khan G.A..,Saw W.G..,...&Gao Y.-G..(2021).Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis.Proceedings of the National Academy of Sciences of the United States of America,118(11).
MLA	Qiao Z.,et al."Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis".Proceedings of the National Academy of Sciences of the United States of America 118.11(2021).