6W8S

Crystal structure of metacaspase 4 from Arabidopsis

6W8S の概要

• エントリーDOI: 10.2210/pdb6w8s/pdb
• 分子名称: Metacaspase-4, SULFATE ION (2 entities in total)
• 機能のキーワード: metacaspase, protease, ca2+-dependent activation, wild-type, plant immunity, plant protein, hydrolase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 187155.74

構造登録者

Zhu, P.,Yu, X.H.,Wang, C.,Zhang, Q.,Liu, W.,McSweeney, S.,Shanklin, J.,Lam, E.,Liu, Q. (登録日: 2020-03-21, 公開日: 2020-05-20, 最終更新日: 2023-10-18)

主引用文献

Zhu, P.,Yu, X.H.,Wang, C.,Zhang, Q.,Liu, W.,McSweeney, S.,Shanklin, J.,Lam, E.,Liu, Q.
Structural basis for Ca2+-dependent activation of a plant metacaspase.
Nat Commun, 11:2249-2249, 2020

PubMed Abstract: Plant metacaspases mediate programmed cell death in development, biotic and abiotic stresses, damage-induced immune response, and resistance to pathogen attack. Most metacaspases require Ca for their activation and substrate processing. However, the Ca-dependent activation mechanism remains elusive. Here we report the crystal structures of Metacaspase 4 from Arabidopsis thaliana (AtMC4) that modulates Ca-dependent, damage-induced plant immune defense. The AtMC4 structure exhibits an inhibitory conformation in which a large linker domain blocks activation and substrate access. In addition, the side chain of Lys225 in the linker domain blocks the active site by sitting directly between two catalytic residues. We show that the activation of AtMC4 and cleavage of its physiological substrate involve multiple cleavages in the linker domain upon activation by Ca. Our analysis provides insight into the Ca-dependent activation of AtMC4 and lays the basis for tuning its activity in response to stresses for engineering of more sustainable crops for food and biofuels.

PubMed: 32382010
DOI: 10.1038/s41467-020-15830-8

実験手法

X-RAY DIFFRACTION (3.484 Å)