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9VBV

Cryo-EM structure of a CARD1 ectodomain H197A/H199A/H222A mutant

Summary for 9VBV
Entry DOI10.2210/pdb9vbv/pdb
EMDB information64934
DescriptorLeucine-rich repeat receptor protein kinase HPCA1,Maltose/maltodextrin-binding periplasmic protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsleucine-rich repeat receptor-like kinase, signaling protein
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains1
Total formula weight101045.95
Authors
Fukuda, Y.,Ishihama, N.,Laohavisit, A. (deposition date: 2025-06-05, release date: 2026-04-08, Last modification date: 2026-06-03)
Primary citationIshihama, N.,Fukuda, Y.,Shirano, Y.,Fujimoto, K.J.,Takizawa, K.,Hiroyama, R.,Ito, H.,Nishimura, M.,Yanai, T.,Inoue, T.,Shirasu, K.,Laohavisit, A.
A copper-dependent redox-based hydrogen peroxide perception in plants.
Nat Commun, 17:-, 2026
Cited by
PubMed Abstract: Redox-related molecules, such as quinones and reactive oxygen species (ROS), are important signaling molecules for all living organisms. A plant-specific leucine-rich repeat receptor-like kinase (LRR-RLK) CANNOT RESPOND TO DMBQ 1 (CARD1), also known as HYDROGEN-PEROXIDE-INDUCED Ca INCREASES (HPCA1), perceives both quinones and ROS, but the mechanism by which it distinguishes between these two types of signals remains unclear. Here, we determine the structure of the CARD1 ectodomain and uncover its unique features. Structural studies, coupled with genetics and biochemical analysis, demonstrate that previously identified unique cysteine residues are not essential for signal perception in CARD1. Interestingly, CARD1 harbors a copper ion on the surface of the ectodomain via histidine-coordination that is crucial for hydrogen peroxide signaling. Our work reports a unique copper-dependent redox perception in plants and provides insight into interactions between receptors and non-peptide stimuli during perception.
PubMed: 42151134
DOI: 10.1038/s41467-026-72573-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.61 Å)
Structure validation

255239

건을2026-06-17부터공개중

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