8Y9O
Crystal structure of AtKAI2 in complex with KK181N1
Summary for 8Y9O
| Entry DOI | 10.2210/pdb8y9o/pdb |
| Descriptor | Probable esterase KAI2, (7-methyl-2,3-dihydroindol-1-yl)-(1,2,3-triazol-1-yl)methanone (3 entities in total) |
| Functional Keywords | atkai2, kk181n1, karrikin-insensitive2, plant hormone receptor, hydrolase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 3 |
| Total formula weight | 92276.64 |
| Authors | Wang, J.W.,Miyakawa, T.,Asami, T. (deposition date: 2024-02-07, release date: 2024-12-04, Last modification date: 2025-01-15) |
| Primary citation | Wang, J.,Takahashi, I.,Kikuzato, K.,Sakai, T.,Zhu, Z.,Jiang, K.,Nakamura, H.,Nakano, T.,Tanokura, M.,Miyakawa, T.,Asami, T. Identification and structure-guided development of triazole urea-based selective antagonists of Arabidopsis karrikin signaling. Nat Commun, 16:104-104, 2025 Cited by PubMed Abstract: The smoke-derived butenolides, karrikins (KARs), regulate many aspects of plant growth and development. However, KARs and a plant hormone, strigolactones (SLs), have high resemblance in signal perception and transduction, making it hard to delineate KARs response due to the shortage of chemical-genetic tools. Here, we identify a triazole urea KK181N1 as an inhibitor of the KARs receptor KAI2. KK181N1 selectively depress the KAR-induced phenotypes in Arabidopsis. We further elucidate the antagonistic, KAI2 binding mechanism of KK181N1, showing that KK181N1 binds to the catalytic pockets of KAI2 in a non-covalent binding manner. Our experiments also demonstrate the binding affinity of triazole urea compounds are regulated by the structured water molecule networks. By fine-tuning this network, we successfully develop a more potent derivative of KK181N1. We anticipate that these chemicals will be applicable to the elucidation of KARs biology, especially for discriminating the molecular and physiological aspects of KARs and SL signaling. PubMed: 39746912DOI: 10.1038/s41467-024-54801-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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