View source for 4l39

==Crystal structure of GH3.12 from Arabidopsis thaliana in complex with AMPCPP and salicylate==
<StructureSection load='4l39' size='340' side='right' caption='[[4l39]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4l39]] is a 2 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=4L39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L39 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4epm|4epm]], [[4ewv|4ewv]], [[4eq4|4eq4]], [[4eql|4eql]]</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 ARATH])</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=4l39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l39 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l39 RCSB], [http://www.ebi.ac.uk/pdbsum/4l39 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 ==
The combination of protein crystallography and small-angle X-ray scattering (SAXS) provides a powerful method to investigate changes in protein conformation. These complementary structural techniques were used to probe the solution structure of the apo and the ligand-bound forms of the Arabidopsis thaliana acyl acid-amido synthetase GH3.12. This enzyme is part of the extensive GH3 family and plays a critical role in the regulation of plant hormones through the formation of amino-acid-conjugated hormone products via an ATP-dependent reaction mechanism. The enzyme adopts two distinct C-terminal domain orientations with `open' and `closed' active sites. Previous studies suggested that ATP only binds in the open orientation. Here, the X-ray crystal structure of GH3.12 is presented in the closed conformation in complex with the nonhydrolysable ATP analogue AMPCPP and the substrate salicylate. Using on-line HPLC purification combined with SAXS measurements, the most likely apo and ATP-bound protein conformations in solution were determined. These studies demonstrate that the C-terminal domain is flexible in the apo form and favours the closed conformation upon ATP binding. In addition, these data illustrate the efficacy of on-line HPLC purification integrated into the SAXS sample-handling environment to reliably monitor small changes in protein conformation through the collection of aggregate-free and highly redundant data.

Determination of the GH3.12 protein conformation through HPLC-integrated SAXS measurements combined with X-ray crystallography.,Round A, Brown E, Marcellin R, Kapp U, Westfall CS, Jez JM, Zubieta C Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2072-80. doi:, 10.1107/S0907444913019276. Epub 2013 Sep 20. PMID:24100325<ref>PMID:24100325</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Brown, E]]
[[Category: Jez, J M]]
[[Category: Kapp, U]]
[[Category: Marcellin, R]]
[[Category: Round, A]]
[[Category: Westfall, C]]
[[Category: Zubieta, C]]
[[Category: Acyl acid amido synthase]]
[[Category: Ligase]]
[[Category: Magnesium]]
[[Category: Protein-ligand complex]]