6LBP

Structure of the Glutamine Phosphoribosylpyrophosphate Amidotransferase from Arabidopsis thaliana

Summary for 6LBP

• Entry DOI: 10.2210/pdb6lbp/pdb
• Descriptor: Amidophosphoribosyltransferase 2, chloroplastic, IRON/SULFUR CLUSTER (2 entities in total)
• Functional Keywords: amidotransferase, tetramer, transferase
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 107388.40

Authors

Yi, Z.,Cao, X.,Han, F.,Feng, Y. (deposition date: 2019-11-14, release date: 2020-04-29, Last modification date: 2023-11-22)

Primary citation

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 FromArabidopsis thaliana.
Front Plant Sci, 11:157-157, 2020

PubMed Abstract: Chloroplastic glutamine phosphoribosylpyrophosphate amidotransferase (GPRATase) catalyzes the first committed step of purine biosynthesis in , 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 and . 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 GPRATases.

PubMed: 32174940
DOI: 10.3389/fpls.2020.00157

Experimental method

X-RAY DIFFRACTION (3.065 Å)