6lbp

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Structure of the Glutamine Phosphoribosylpyrophosphate Amidotransferase from Arabidopsis thalianaStructure of the Glutamine Phosphoribosylpyrophosphate Amidotransferase from Arabidopsis thaliana

Structural highlights

6lbp is a 2 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 3.065Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASE2_ARATH Catalyzes the first committed step of 'de novo purine biosynthesis from glutamine. Required for chloroplast biogenesis and cell division. Confers sensitivity to the phenyltriazole acetic acid compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid (DAS734), a bleaching herbicide.[1] [2] [3]

Publication Abstract from PubMed

Chloroplastic glutamine phosphoribosylpyrophosphate amidotransferase (GPRATase) catalyzes the first committed step of de novo purine biosynthesis in Arabidopsis thaliana, and DAS734 is a direct and specific inhibitor of AtGPRAT, with phytotoxic effects similar to the leaf beaching phenotypes of known AtGPRAT genetic mutants, especially cia1 and atd2. However, the structure of AtGPRAT and the inhibition mode of DAS734 still remain poorly understood. In this study, we solved the structure of AtGPRAT2, which revealed structural differences between AtGPRAT2 and bacterial enzymes. Kinetics assay demonstrated that DAS734 behaves as a competitive inhibitor for the substrate phosphoribosyl pyrophosphate (PRPP) of AtGPRAT2. Docking studies showed that DAS734 forms electrostatic interactions with R264 and hydrophobic interactions with several residues, which was verified by binding assays. Collectively, our study provides important insights into the inhibition mechanism of DAS734 to AtGPRAT2 and sheds light on future studies into further development of more potent herbicides targeting Arabidopsis GPRATases.

Crystal Structure of the Chloroplastic Glutamine Phosphoribosylpyrophosphate Amidotransferase GPRAT2 From Arabidopsis thaliana.,Cao X, Du B, Han F, Zhou Y, Ren J, Wang W, Chen Z, Zhang Y Front Plant Sci. 2020 Feb 27;11:157. doi: 10.3389/fpls.2020.00157. eCollection, 2020. PMID:32174940[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ van der Graaff E, Hooykaas P, Lein W, Lerchl J, Kunze G, Sonnewald U, Boldt R. Molecular analysis of "de novo" purine biosynthesis in solanaceous species and in Arabidopsis thaliana. Front Biosci. 2004 May 1;9:1803-16. PMID:14977588 doi:10.2741/1344
  2. ↑ Hung WF, Chen LJ, Boldt R, Sun CW, Li HM. Characterization of Arabidopsis glutamine phosphoribosyl pyrophosphate amidotransferase-deficient mutants. Plant Physiol. 2004 Jul;135(3):1314-23. PMID:15266056 doi:10.1104/pp.104.040956
  3. ↑ Walsh TA, Bauer T, Neal R, Merlo AO, Schmitzer PR, Hicks GR, Honma M, Matsumura W, Wolff K, Davies JP. Chemical genetic identification of glutamine phosphoribosylpyrophosphate amidotransferase as the target for a novel bleaching herbicide in Arabidopsis. Plant Physiol. 2007 Jul;144(3):1292-304. PMID:17616508 doi:10.1104/pp.107.099705
  4. ↑ Cao X, Du B, Han F, Zhou Y, Ren J, Wang W, Chen Z, Zhang Y. Crystal Structure of the Chloroplastic Glutamine Phosphoribosylpyrophosphate Amidotransferase GPRAT2 From Arabidopsis thaliana. Front Plant Sci. 2020 Feb 27;11:157. PMID:32174940 doi:10.3389/fpls.2020.00157

6lbp, resolution 3.06Å

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