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[[Image:1pmo.gif|left|200px]]


{{Structure
==Crystal structure of Escherichia coli GadB (neutral pH)==
|PDB= 1pmo |SIZE=350|CAPTION= <scene name='initialview01'>1pmo</scene>, resolution 2.3&Aring;
<StructureSection load='1pmo' size='340' side='right'caption='[[1pmo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
<table><tr><td colspan='2'>[[1pmo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PMO FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE= GADB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmo OCA], [https://pdbe.org/1pmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pmo RCSB], [https://www.ebi.ac.uk/pdbsum/1pmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pmo ProSAT]</span></td></tr>
|RELATEDENTRY=[[1pmm|1PMM]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmo OCA], [http://www.ebi.ac.uk/pdbsum/1pmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pmo RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/DCEB_ECOLI DCEB_ECOLI]
 
== Evolutionary Conservation ==
'''Crystal structure of Escherichia coli GadB (neutral pH)'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pm/1pmo_consurf.spt"</scriptWhenChecked>
Glutamate decarboxylase is a vitamin B6-dependent enzyme, which catalyses the decarboxylation of glutamate to gamma-aminobutyrate. In Escherichia coli, expression of glutamate decarboxylase (GadB), a 330 kDa hexamer, is induced to maintain the physiological pH under acidic conditions, like those of the passage through the stomach en route to the intestine. GadB, together with the antiporter GadC, constitutes the gad acid resistance system, which confers the ability for bacterial survival for at least 2 h in a strongly acidic environment. GadB undergoes a pH-dependent conformational change and exhibits an activity optimum at low pH. We determined the crystal structures of GadB at acidic and neutral pH. They reveal the molecular details of the conformational change and the structural basis for the acidic pH optimum. We demonstrate that the enzyme is localized exclusively in the cytoplasm at neutral pH, but is recruited to the membrane when the pH falls. We show by structure-based site-directed mutagenesis that the triple helix bundle formed by the N-termini of the protein at acidic pH is the major determinant for this behaviour.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1PMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMO OCA].  
</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/main_output.php?pdb_ID=1pmo ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase., Capitani G, De Biase D, Aurizi C, Gut H, Bossa F, Grutter MG, EMBO J. 2003 Aug 15;22(16):4027-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12912902 12912902]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamate decarboxylase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Aurizi C]]
[[Category: Aurizi, C.]]
[[Category: Bossa F]]
[[Category: Biase, D De.]]
[[Category: Capitani G]]
[[Category: Bossa, F.]]
[[Category: De Biase D]]
[[Category: Capitani, G.]]
[[Category: Grutter MG]]
[[Category: Grutter, M G.]]
[[Category: Gut H]]
[[Category: Gut, H.]]
[[Category: neutral-ph form of gadb]]
 
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Retrieved from "https://proteopedia.org/1pmo"