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| | <StructureSection load='3hbx' size='340' side='right'caption='[[3hbx]], [[Resolution|resolution]] 2.67Å' scene=''> | | <StructureSection load='3hbx' size='340' side='right'caption='[[3hbx]], [[Resolution|resolution]] 2.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hbx]] is a 6 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=3HBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HBX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hbx]] is a 6 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=3HBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.672Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g17330, GAD, GAD1, GDH1, MKP11.30, MKP11_18 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate_decarboxylase Glutamate decarboxylase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3hbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hbx OCA], [https://pdbe.org/3hbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hbx RCSB], [https://www.ebi.ac.uk/pdbsum/3hbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hbx ProSAT]</span></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=3hbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hbx OCA], [https://pdbe.org/3hbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hbx RCSB], [https://www.ebi.ac.uk/pdbsum/3hbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hbx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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>
| + | [https://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Glutamate decarboxylase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Capitani, G]] | + | [[Category: Capitani G]] |
| - | [[Category: Dominici, P]] | + | [[Category: Dominici P]] |
| - | [[Category: Gruetter, M G]] | + | [[Category: Gruetter MG]] |
| - | [[Category: Gut, H]] | + | [[Category: Gut H]] |
| - | [[Category: Pilati, S]] | + | [[Category: Pilati S]] |
| - | [[Category: Calmodulin-binding]]
| + | |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zik M, Arazi T, Snedden WA, Fromm H. Two isoforms of glutamate decarboxylase in Arabidopsis are regulated by calcium/calmodulin and differ in organ distribution. Plant Mol Biol. 1998 Aug;37(6):967-75. PMID:9700069
- ↑ Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grutter MG, Capitani G. A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. J Mol Biol. 2009 Sep 18;392(2):334-51. Epub 2009 Jul 4. PMID:19580813 doi:10.1016/j.jmb.2009.06.080
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