Structure-guided Analysis of the Arabidopsis JASMONATE-INDUCED OXYGENASE (JOX) 2 Reveals Key Residues of Plant JOX Recognizing Jasmonic Acid Substrate

编号 040028102

推送时间 20210308

研究领域 森林培育 

年份 2021 

类型 期刊 

语种 英语

标题 Structure-guided Analysis of the Arabidopsis JASMONATE-INDUCED OXYGENASE (JOX) 2 Reveals Key Residues of Plant JOX Recognizing Jasmonic Acid Substrate

来源期刊 Molecular Plant

期 第281期

发表时间 20210127

关键词 crystal structure;  JASMONATE-INDUCED OXYGENASEs (JOXs);  jasmonic acid (JA);  12-OHJA;  hydroxylation; 

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

服务人员 孙小满

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