6lsv

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==Crystal structure of JOX2 in complex with 2OG, Fe, and JA==
==Crystal structure of JOX2 in complex with 2OG, Fe, and JA==
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<StructureSection load='6lsv' size='340' side='right'caption='[[6lsv]]' scene=''>
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<StructureSection load='6lsv' size='340' side='right'caption='[[6lsv]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LSV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6lsv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LSV FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lsv OCA], [https://pdbe.org/6lsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lsv RCSB], [https://www.ebi.ac.uk/pdbsum/6lsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lsv ProSAT]</span></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=JAA:{(1R,2R)-3-OXO-2-[(2Z)-PENT-2-EN-1-YL]CYCLOPENTYL}ACETIC+ACID'>JAA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g05600, MOP10.14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lsv OCA], [https://pdbe.org/6lsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lsv RCSB], [https://www.ebi.ac.uk/pdbsum/6lsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lsv ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/DIOX5_ARATH DIOX5_ARATH]] Involved in anthocyanin and protoanthocyanidin biosynthesis by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins (By similarity). May be involved in the catabolism of cytotoxic polycyclic aromatic hydrocarbons (PAHs) (PubMed:27637093).[UniProtKB:Q96323]<ref>PMID:27637093</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 A 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 beta helix (DSBH) core flanked by alpha 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.
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Structure-guided analysis of Arabidopsis JASMONATE-INDUCED OXYGENASE (JOX) 2 reveals key residues for recognition of jasmonic acid substrate by plant JOXs.,Zhang X, Wang D, Elberse J, Qi L, Shi W, Peng YL, Schuurink RC, Van den Ackerveken G, Liu J Mol Plant. 2021 May 3;14(5):820-828. doi: 10.1016/j.molp.2021.01.017. Epub 2021, Jan 28. PMID:33516967<ref>PMID:33516967</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6lsv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Liu J]]
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[[Category: Liu, J]]
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[[Category: Wang D]]
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[[Category: Wang, D]]
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[[Category: Zhang X]]
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[[Category: Zhang, X]]
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[[Category: 2og oxygenase]]
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[[Category: Jasmonic acid]]
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[[Category: Plant protein]]

Revision as of 09:34, 12 May 2021

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

PDB ID 6lsv

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