6e1q

AtGH3.15 acyl acid amido synthetase in complex with 2,4-DB

spinqualitylabelsall models 6e1q, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6e1q is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.148Å Ligands: CFA, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GH315_ARATH Indole-3-acetic acid-amido (IAA) synthetase that catalyzes the conjugation of amino acids to auxin specifically using the auxin precursor indole-3-butyric acid (IBA) and glutamine and, possibly, cysteine as substrates (PubMed:29462792, PubMed:30315112). Displays high catalytic activity with the auxinic phenoxyalkanoic acid herbicides 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and to some extent 2,4-dichlorophenoxylacetic acid (2,4-D) as substrates, thus confering resistance to herbicides (PubMed:30315112). Publication Abstract from PubMed Herbicide-resistance traits are the most widely used agriculture biotechnology products. Yet, to maintain their effectiveness and to mitigate selection of herbicide-resistant weeds, the discovery of new resistance traits that use different chemical modes of action is essential. In plants, the Gretchen Hagen 3 (GH3) acyl acid amido synthetases catalyze the conjugation of amino acids to jasmonate and auxin phytohormones. This reaction chemistry has not been explored as a possible approach for herbicide modification and inactivation. Here, we examined a set of Arabidopsis GH3 proteins that use the auxins indole-3-acetic acid (IAA) and indole-3-butyric acid (IBA) as substrates along with the corresponding auxinic phenoxyalkanoic acid herbicides 2,4-dichlorophenoxylacetic acid (2,4-D) and 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB). The IBA-specific AtGH3.15 protein displayed high catalytic activity with 2,4-DB, which was comparable to its activity with IBA. Screening of phenoxyalkanoic and phenylalkyl acids indicated that side-chain length of alkanoic and alkyl acids is a key feature of AtGH3.15's substrate preference. The X-ray crystal structure of the AtGH3.15*2,4-DB complex revealed how the herbicide binds in the active site. In root elongation assays, Arabidopsis AtGH3.15-knockout and -overexpression lines grown in the presence of 2,4-DB exhibited hypersensitivity and tolerance, respectively, indicating that the AtGH3.15-catalyzed modification inactivates 2,4-DB. These findings suggest a potential use for AtGH3.15, and perhaps other GH3 proteins, as herbicide-modifying enzymes that employ a mode of action different from those of currently available herbicide resistance traits. Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis.,Sherp AM, Lee SG, Schraft E, Jez JM J Biol Chem. 2018 Oct 12. pii: RA118.004975. doi: 10.1074/jbc.RA118.004975. PMID:30315112 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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