7mds | pdb_00007mds

Crystal structure of AtDHDPS1 in complex with MBDTA-2

spinqualitylabelsall models 7mds, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.295Å Ligands: CL, YXP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Weeds are becoming increasingly resistant to our current herbicides, posing a significant threat to agricultural production. Therefore, new herbicides with novel modes of action are urgently needed. In this study, we exploited a novel herbicide target, dihydrodipicolinate synthase (DHDPS), which catalyses the first and rate-limiting step in lysine biosynthesis. The first class of plant DHDPS inhibitors with micromolar potency against Arabidopsis thaliana DHDPS were identified using a high throughput chemical screen. We determined that this class of inhibitors binds to a novel and unexplored pocket within DHDPS, which is highly conserved across plant species. The inhibitors also attenuated the germination and growth of A. thaliana seedlings and confirmed their pre-emergence herbicidal activity in soil-grown plants. These results provide proof-of-concept that lysine biosynthesis represents a promising target for the development of herbicides with a novel mode of action to tackle the global rise of herbicide resistant weeds. Towards novel herbicide modes of action by inhibiting lysine biosynthesis in plants.,Soares da Costa TP, Hall CJ, Panjikar S, Wyllie JA, Christoff RM, Bayat S, Hulett MD, Abbott BM, Gendall AR, Perugini MA Elife. 2021 Jul 27;10. pii: 69444. doi: 10.7554/eLife.69444. PMID:34313586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dihydrodipicolinate synthase

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