7CK1

Crystal structure of arabidopsis CESA3 catalytic domain

7CK1 の概要

• エントリーDOI: 10.2210/pdb7ck1/pdb
• 分子名称: Cellulose synthase A catalytic subunit 3 [UDP-forming],Cellulose synthase A catalytic subunit 3 [UDP-forming], MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: enzyme, synthase, plant protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92052.42

構造登録者

Qiao, Z.,Gao, Y.G. (登録日: 2020-07-15, 公開日: 2021-03-17, 最終更新日: 2021-03-31)

主引用文献

Qiao, Z.,Lampugnani, E.R.,Yan, X.F.,Khan, G.A.,Saw, W.G.,Hannah, P.,Qian, F.,Calabria, J.,Miao, Y.,Gruber, G.,Persson, S.,Gao, Y.G.
Structure of Arabidopsis CESA3 catalytic domain with its substrate UDP-glucose provides insight into the mechanism of cellulose synthesis.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Cellulose is synthesized by cellulose synthases (CESAs) from the glycosyltransferase GT-2 family. In plants, the CESAs form a six-lobed rosette-shaped CESA complex (CSC). Here we report crystal structures of the catalytic domain of CESA3 (AtCESA3) in both apo and uridine diphosphate (UDP)-glucose (UDP-Glc)-bound forms. AtCESA3 has 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 AtCESA3 onto 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 AtCESA3 can 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 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 CESAs might dimerize to eventually assemble into CSCs in plants.

PubMed: 33729990
DOI: 10.1073/pnas.2024015118

実験手法

X-RAY DIFFRACTION (2.35 Å)