9IX7
Crystal structure of homolog of dihydroxyacid dehydratase(AstD) from Aspergillus terreus
Summary for 9IX7
| Entry DOI | 10.2210/pdb9ix7/pdb |
| Descriptor | dihydroxy-acid dehydratase, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | dihydroxyacid dehydratase, lyase |
| Biological source | Aspergillus terreus |
| Total number of polymer chains | 2 |
| Total formula weight | 120683.94 |
| Authors | |
| Primary citation | Zang, X.,Bat-Erdene, U.,Huang, W.,Wu, Z.,Jacobsen, S.E.,Tang, Y.,Zhou, J. Structural Bases of Dihydroxy Acid Dehydratase Inhibition and Biodesign for Self-Resistance. Biodes Res, 6:0046-0046, 2024 Cited by PubMed Abstract: Dihydroxy acid dehydratase (DHAD) is the third enzyme in the plant branched-chain amino acid biosynthetic pathway and the target for commercial herbicide development. We have previously reported the discovery of fungal natural product aspterric acid (AA) as a submicromolar inhibitor of DHAD through self-resistance gene directed genome mining. Here, we reveal the mechanism of AA inhibition on DHAD and the self-resistance mechanism of AstD, which is encoded by the self-resistance gene D. As a competitive inhibitor, the hydroxycarboxylic acid group of AA mimics the binding of the natural substrate of DHAD, while the hydrophobic moiety of AA occupies the substrate entrance cavity. Compared to DHAD, AstD has a relatively narrow substrate channel to prevent AA from binding. Several mutants of DHAD were generated and assayed to validate the self-resistance mechanism and to confer DHAD with AA resistance. These results will lead to the engineering of new type of herbicides targeting DHAD and provide direction for the ecological construction of herbicide-resistant crops. PubMed: 39494391DOI: 10.34133/bdr.0046 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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