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{{STRUCTURE_3hbx| PDB=3hbx | SCENE= }}
==Crystal structure of GAD1 from Arabidopsis thaliana==
===Crystal structure of GAD1 from Arabidopsis thaliana===
<StructureSection load='3hbx' size='340' side='right' caption='[[3hbx]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
{{ABSTRACT_PUBMED_19580813}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3hbx]] is a 6 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=3HBX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HBX FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g17330, GAD, GAD1, GDH1, MKP11.30, MKP11_18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_decarboxylase Glutamate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.15 4.1.1.15] </span></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=3hbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hbx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hbx RCSB], [http://www.ebi.ac.uk/pdbsum/3hbx PDBsum]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hb/3hbx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutamate decarboxylase (Gad) catalyzes glutamate to gamma-aminobutyrate conversion. Plant Gad is a approximately 340 kDa hexamer, involved in development and stress response, and regulated by pH and binding of Ca(2+)/calmodulin (CaM) to the C-terminal domain. We determined the crystal structure of Arabidopsis thaliana Gad1 in its CaM-free state, obtained a low-resolution structure of the calmodulin-activated Gad complex by small-angle X-ray scattering and identified the crucial residues, in the C-terminal domain, for regulation by pH and CaM binding. CaM activates Gad1 in a unique way by relieving two C-terminal autoinhibition domains of adjacent active sites, forming a 393 kDa Gad1-CaM complex with an unusual 1:3 stoichiometry. The complex is loosely packed: thanks to the flexible linkers connecting the enzyme core with the six C-terminal regulatory domains, the CaM molecules retain considerable positional and orientational freedom with respect to Gad1. The complex thus represents a prototype for a novel CaM-target interaction mode. Thanks to its two levels of regulation, both targeting the C-terminal domain, Gad can respond flexibly to different kinds of cellular stress occurring at different pH values.


==Function==
A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase.,Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grutter MG, Capitani G J Mol Biol. 2009 Sep 18;392(2):334-51. Epub 2009 Jul 4. PMID:19580813<ref>PMID:19580813</ref>
[[http://www.uniprot.org/uniprot/DCE1_ARATH DCE1_ARATH]] Catalyzes the production of GABA. The calmodulin-binding is calcium-dependent and it is proposed that this may, directly or indirectly, form a calcium regulated control of GABA biosynthesis.<ref>PMID:9700069</ref>  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3hbx]] is a 6 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=3HBX OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019580813</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Glutamate decarboxylase]]
[[Category: Glutamate decarboxylase]]
[[Category: Capitani, G.]]
[[Category: Capitani, G]]
[[Category: Dominici, P.]]
[[Category: Dominici, P]]
[[Category: Gruetter, M G.]]
[[Category: Gruetter, M G]]
[[Category: Gut, H.]]
[[Category: Gut, H]]
[[Category: Pilati, S.]]
[[Category: Pilati, S]]
[[Category: Calmodulin-binding]]
[[Category: Calmodulin-binding]]
[[Category: Decarboxylase]]
[[Category: Decarboxylase]]
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Pyridoxal phosphate]]
[[Category: Pyridoxal phosphate]]
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