7VKA
Crystal Structure of GH3.6 in complex with an inhibitor
Summary for 7VKA
| Entry DOI | 10.2210/pdb7vka/pdb |
| Descriptor | Indole-3-acetic acid-amido synthetase GH3.6, ADENOSINE MONOPHOSPHATE, N-[4-[(6-chloranylpyridazin-3-yl)amino]phenyl]-3-(trifluoromethyl)benzamide, ... (5 entities in total) |
| Functional Keywords | inhibitor, complex, ligase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 139686.76 |
| Authors | |
| Primary citation | Xie, Y.,Zhu, Y.,Wang, N.,Luo, M.,Ota, T.,Guo, R.,Takahashi, I.,Yu, Z.,Aizezi, Y.,Zhang, L.,Yan, Y.,Zhang, Y.,Bao, H.,Wang, Y.,Zhu, Z.,Huang, A.C.,Zhao, Y.,Asami, T.,Huang, H.,Guo, H.,Jiang, K. Chemical genetic screening identifies nalacin as an inhibitor of GH3 amido synthetase for auxin conjugation. Proc.Natl.Acad.Sci.USA, 119:e2209256119-e2209256119, 2022 Cited by PubMed Abstract: Auxin inactivation is critical for plant growth and development. To develop plant growth regulators functioning in auxin inactivation pathway, we performed a phenotype-based chemical screen in Arabidopsis and identified a chemical, nalacin, that partially mimicked the effects of auxin. Genetic, pharmacological, and biochemical approaches demonstrated that nalacin exerts its auxin-like activities by inhibiting indole-3-acetic acid (IAA) conjugation that is mediated by Gretchen Hagen 3 (GH3) acyl acid amido synthetases. The crystal structure of Arabidopsis GH3.6 in complex with D4 (a derivative of nalacin) together with docking simulation analysis revealed the molecular basis of the inhibition of group II GH3 by nalacin. Sequence alignment analysis indicated broad bioactivities of nalacin and D4 as inhibitors of GH3s in vascular plants, which were confirmed, at least, in tomato and rice. In summary, our work identifies nalacin as a potent inhibitor of IAA conjugation mediated by group II GH3 that plays versatile roles in hormone-regulated plant development and has potential applications in both basic research and agriculture. PubMed: 36454752DOI: 10.1073/pnas.2209256119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.401 Å) |
Structure validation
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