3vp6
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Structural characterization of Glutamic Acid Decarboxylase; insights into the mechanism of autoinactivation== | |
| - | + | <StructureSection load='3vp6' size='340' side='right' caption='[[3vp6]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3vp6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteroides_caccae Bacteroides caccae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VP6 FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HLD:4-OXO-4H-PYRAN-2,6-DICARBOXYLIC+ACID'>HLD</scene></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">GAD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47678 Bacteroides caccae])</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=3vp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vp6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vp6 RCSB], [http://www.ebi.ac.uk/pdbsum/3vp6 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
[[http://www.uniprot.org/uniprot/DCE1_HUMAN DCE1_HUMAN]] Defects in GAD1 are the cause of cerebral palsy spastic quadriplegic type 1 (CPSQ1) [MIM:[http://omim.org/entry/603513 603513]]. A non-progressive disorder of movement and/or posture resulting from defects in the developing central nervous system. Affected individuals manifest symmetrical, non-progressive spasticity and no adverse perinatal history or obvious underlying alternative diagnosis. Developmental delay, mental retardation and sometimes epilepsy can be part of the clinical picture.<ref>PMID:15571623</ref> | [[http://www.uniprot.org/uniprot/DCE1_HUMAN DCE1_HUMAN]] Defects in GAD1 are the cause of cerebral palsy spastic quadriplegic type 1 (CPSQ1) [MIM:[http://omim.org/entry/603513 603513]]. A non-progressive disorder of movement and/or posture resulting from defects in the developing central nervous system. Affected individuals manifest symmetrical, non-progressive spasticity and no adverse perinatal history or obvious underlying alternative diagnosis. Developmental delay, mental retardation and sometimes epilepsy can be part of the clinical picture.<ref>PMID:15571623</ref> | ||
| - | + | == Function == | |
| - | ==Function== | + | |
[[http://www.uniprot.org/uniprot/DCE1_HUMAN DCE1_HUMAN]] Catalyzes the production of GABA. | [[http://www.uniprot.org/uniprot/DCE1_HUMAN DCE1_HUMAN]] Catalyzes the production of GABA. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Imbalances in GABA homeostasis underlie psychiatric and movement disorders. The ability of the 65kDa isoform of glutamic acid decarboxylase, GAD65, to control synaptic GABA levels is influenced through its capacity to auto-inactivate. In contrast, the GAD67 isoform is constitutively active. Previous structural insights suggest that flexibility in the GAD65 catalytic loop drives enzyme inactivation. To test this idea, we constructed a panel of GAD65/67 chimeras and compared the ability of these molecules to auto-inactivate. Together, our data reveal the important finding that the C-terminal domain of GAD plays a key role in controlling GAD65 auto-inactivation. In support of these findings, we determined the X-ray crystal structure of a GAD65/67 chimera that reveals the conformation of the catalytic loop is intimately linked to the C-terminal domain. | ||
| - | + | Structural characterization on the mechanism of auto-inactivation for Human Glutamic Acid Decarboxylase.,Langendorf CG, Tuck KL, Key TL, Fenalti G, Pike RN, Rosado CJ, Wong AS, Buckle AM, Law RH, Whisstock JC Biosci Rep. 2012 Nov 5. PMID:23126365<ref>PMID:23126365</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bacteroides caccae]] | [[Category: Bacteroides caccae]] | ||
[[Category: Glutamate decarboxylase]] | [[Category: Glutamate decarboxylase]] | ||
| - | [[Category: Buckle, A M | + | [[Category: Buckle, A M]] |
| - | [[Category: Fenalti, G | + | [[Category: Fenalti, G]] |
| - | [[Category: Key, T L.G | + | [[Category: Key, T L.G]] |
| - | [[Category: Langendorf, C G | + | [[Category: Langendorf, C G]] |
| - | [[Category: Law, R H.P | + | [[Category: Law, R H.P]] |
| - | [[Category: Rosado, C J | + | [[Category: Rosado, C J]] |
| - | [[Category: Tuck, K L | + | [[Category: Tuck, K L]] |
| - | [[Category: Whisstock, J C | + | [[Category: Whisstock, J C]] |
| - | [[Category: Wong, A S.M | + | [[Category: Wong, A S.M]] |
[[Category: Catalytic loop swap]] | [[Category: Catalytic loop swap]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 06:31, 21 December 2014
Structural characterization of Glutamic Acid Decarboxylase; insights into the mechanism of autoinactivation
| |||||||||||
