6w8s | pdb_00006w8s
Crystal structure of metacaspase 4 from Arabidopsis
Structural highlights
FunctionMCA4_ARATH Cysteine protease that cleaves specifically after arginine or lysine residues. Does not cleave caspase-specific substrates. Plays a positive regulatory role in biotic and abiotic stress-induced programmed cell death.[1] [2] [3] Publication Abstract from PubMedPlant metacaspases mediate programmed cell death in development, biotic and abiotic stresses, damage-induced immune response, and resistance to pathogen attack. Most metacaspases require Ca(2+) for their activation and substrate processing. However, the Ca(2+)-dependent activation mechanism remains elusive. Here we report the crystal structures of Metacaspase 4 from Arabidopsis thaliana (AtMC4) that modulates Ca(2+)-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(2+). Our analysis provides insight into the Ca(2+)-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. Structural basis for Ca(2+)-dependent activation of a plant metacaspase.,Zhu P, Yu XH, Wang C, Zhang Q, Liu W, McSweeney S, Shanklin J, Lam E, Liu Q Nat Commun. 2020 May 7;11(1):2249. doi: 10.1038/s41467-020-15830-8. PMID:32382010[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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