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4epm
From Proteopedia
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| - | [[ | + | ==Crystal Structure of Arabidopsis GH3.12 (PBS3) in Complex with AMP== |
| + | <StructureSection load='4epm' size='340' side='right' caption='[[4epm]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4epm]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EPM FirstGlance]. <br> | ||
| + | </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> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4epl|4epl]], [[4eql|4eql]], [[4ewv|4ewv]]</td></tr> | ||
| + | <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 Arabidopsis thaliana])</td></tr> | ||
| + | <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://www.rcsb.org/pdb/explore.do?structureId=4epm RCSB], [http://www.ebi.ac.uk/pdbsum/4epm PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
| - | [[Category: Herrmann, J | + | [[Category: Herrmann, J]] |
| - | [[Category: Jez, J M | + | [[Category: Jez, J M]] |
| - | [[Category: Kapp, U | + | [[Category: Kapp, U]] |
| - | [[Category: Nanao, M H | + | [[Category: Nanao, M H]] |
| - | [[Category: Westfall, C S | + | [[Category: Westfall, C S]] |
| - | [[Category: Zubieta, C | + | [[Category: Zubieta, C]] |
[[Category: Acyl acid-amido synthetase]] | [[Category: Acyl acid-amido synthetase]] | ||
[[Category: Adenylation]] | [[Category: Adenylation]] | ||
[[Category: Anl superfamily]] | [[Category: Anl superfamily]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
Revision as of 11:09, 25 December 2014
Crystal Structure of Arabidopsis GH3.12 (PBS3) in Complex with AMP
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