6LSV

Crystal structure of JOX2 in complex with 2OG, Fe, and JA

Summary for 6LSV

• Entry DOI: 10.2210/pdb6lsv/pdb
• Descriptor: Probable 2-oxoglutarate-dependent dioxygenase At5g05600, 2-OXOGLUTARIC ACID, {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid, ... (5 entities in total)
• Functional Keywords: jasmonic acid, 2og oxygenase, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 81066.84

Authors

Zhang, X.,Wang, D.,Liu, J. (deposition date: 2020-01-20, release date: 2021-02-10, Last modification date: 2023-11-29)

Primary citation

Zhang, X.,Wang, D.,Elberse, J.,Qi, L.,Shi, W.,Peng, Y.L.,Schuurink, R.C.,Van den Ackerveken, G.,Liu, J.
Structure-guided analysis of Arabidopsis JASMONATE-INDUCED OXYGENASE (JOX) 2 reveals key residues for recognition of jasmonic acid substrate by plant JOXs.
Mol Plant, 14:820-828, 2021

PubMed Abstract: The jasmonic acid (JA) signaling pathway is used by plants to control wound responses. The persistent accumulation of JA inhibits plant growth, and the hydroxylation of JA to 12-hydroxy-JA by JASMONATE-INDUCED OXYGENASEs (JOXs, also named jasmonic acid oxidases) is therefore vital for plant growth, while structural details of JA recognition by JOXs are unknown. Here, we present the 2.65 Å resolution X-ray crystal structure of Arabidopsis JOX2 in complex with its substrate JA and its co-substrates 2-oxoglutarate and Fe(II). JOX2 contains a distorted double-stranded β helix (DSBH) core flanked by α helices and loops. JA is bound in the narrow substrate pocket by hydrogen bonds with the arginine triad R225, R350, and R354 and by hydrophobic interactions mainly with the phenylalanine triad F157, F317, and F346. The most critical residues for JA binding are F157 and R225, both from the DSBH core, which interact with the cyclopentane ring of JA. The spatial distribution of critical residues for JA binding and the shape of the substrate-binding pocket together define the substrate selectivity of the JOXs. Sequence alignment shows that these critical residues are conserved among JOXs from higher plants. Collectively, our study provides insights into the mechanism by which higher plants hydroxylate the hormone JA.

PubMed: 33516967
DOI: 10.1016/j.molp.2021.01.017

Experimental method

X-RAY DIFFRACTION (2.651 Å)