4epm

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==Crystal Structure of Arabidopsis GH3.12 (PBS3) in Complex with AMP==
==Crystal Structure of Arabidopsis GH3.12 (PBS3) in Complex with AMP==
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<StructureSection load='4epm' size='340' side='right' caption='[[4epm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='4epm' size='340' side='right'caption='[[4epm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4epm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EPM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EPM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4epm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EPM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.099&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4epl|4epl]], [[4eql|4eql]], [[4ewv|4ewv]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GH3.12, GDG1, PBS3, WIN3, At5g13320, T22N19.5, T31B5.140 ([http://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=4epm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4epm OCA], [https://pdbe.org/4epm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4epm RCSB], [https://www.ebi.ac.uk/pdbsum/4epm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4epm ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4epm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4epm OCA], [http://pdbe.org/4epm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4epm RCSB], [http://www.ebi.ac.uk/pdbsum/4epm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4epm ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GH312_ARATH GH312_ARATH]] Catalyzes the conjugation of specific amino acids (e.g. Glu and possibly His, Lys, and Met) to their preferred acyl substrates (e.g. 4-substituted benzoates), in a magnesium ion- and ATP-dependent manner. Can use 4-substituted benzoates such as 4-aminobenzoate (pABA), 4-fluorobenzoate and 4-hydroxybenzoate (4-HBA), and, to a lesser extent, benzoate, vanillate and trans-cinnamate, but not 2-substituted benzoates and salicylic acid (SA), as conjugating acyl substrates. Involved in both basal and induced resistance in a SA-dependent manner. Confers resistance to virulent and avirulent pathogens (at least bacteria and oomycetes), and promotes SA glucosides accumulation. Required for the establishment of hyper-sensitive response (HR) upon incompatible interaction and subsequent systemic acquired resistance (SAR).<ref>PMID:18266921</ref> <ref>PMID:10224270</ref> <ref>PMID:11846877</ref> <ref>PMID:16353557</ref> <ref>PMID:17918621</ref> <ref>PMID:17521413</ref> <ref>PMID:17468220</ref> <ref>PMID:19189963</ref>
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[https://www.uniprot.org/uniprot/GH312_ARATH GH312_ARATH] Catalyzes the conjugation of specific amino acids (e.g. Glu and possibly His, Lys, and Met) to their preferred acyl substrates (e.g. 4-substituted benzoates), in a magnesium ion- and ATP-dependent manner. Can use 4-substituted benzoates such as 4-aminobenzoate (pABA), 4-fluorobenzoate and 4-hydroxybenzoate (4-HBA), and, to a lesser extent, benzoate, vanillate and trans-cinnamate, but not 2-substituted benzoates and salicylic acid (SA), as conjugating acyl substrates. Involved in both basal and induced resistance in a SA-dependent manner. Confers resistance to virulent and avirulent pathogens (at least bacteria and oomycetes), and promotes SA glucosides accumulation. Required for the establishment of hyper-sensitive response (HR) upon incompatible interaction and subsequent systemic acquired resistance (SAR).<ref>PMID:18266921</ref> <ref>PMID:10224270</ref> <ref>PMID:11846877</ref> <ref>PMID:16353557</ref> <ref>PMID:17918621</ref> <ref>PMID:17521413</ref> <ref>PMID:17468220</ref> <ref>PMID:19189963</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acyl acid amido synthetases of the GH3 family act as critical prereceptor modulators of plant hormone action; however, the molecular basis for their hormone selectivity is unclear. Here, we report the crystal structures of benzoate-specific Arabidopsis thaliana AtGH3.12/PBS3 and jasmonic acid (JA)-specific AtGH3.11/JAR1. These structures, combined with biochemical analysis, define features for the conjugation of amino acids to diverse acyl acid substrates and highlight the importance of conformational changes in the C-terminal domain for catalysis. We also identify residues forming the acyl acid binding site across the GH3 family and residues critical for amino acid recognition. Our results demonstrate how a highly adaptable three-dimensional scaffold is used for the evolution of promiscuous activity across an enzyme family for modulation of plant signaling molecules.
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Structural Basis for Prereceptor Modulation of Plant Hormones by GH3 Proteins.,Westfall CS, Zubieta C, Herrmann J, Kapp U, Nanao MH, Jez JM Science. 2012 May 24. PMID:22628555<ref>PMID:22628555</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 4epm" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Herrmann, J]]
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[[Category: Large Structures]]
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[[Category: Jez, J M]]
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[[Category: Herrmann J]]
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[[Category: Kapp, U]]
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[[Category: Jez JM]]
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[[Category: Nanao, M H]]
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[[Category: Kapp U]]
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[[Category: Westfall, C S]]
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[[Category: Nanao MH]]
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[[Category: Zubieta, C]]
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[[Category: Westfall CS]]
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[[Category: Acyl acid-amido synthetase]]
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[[Category: Zubieta C]]
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[[Category: Adenylation]]
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[[Category: Anl superfamily]]
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[[Category: Ligase]]
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Current revision

Crystal Structure of Arabidopsis GH3.12 (PBS3) in Complex with AMP

PDB ID 4epm

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