2dgm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(6 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2dgm.png|left|200px]]


{{STRUCTURE_2dgm| PDB=2dgm | SCENE= }}
==Crystal structure of Escherichia coli GadB in complex with iodide==
<StructureSection load='2dgm' size='340' side='right'caption='[[2dgm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dgm]] 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=2DGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DGM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=2dgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dgm OCA], [https://pdbe.org/2dgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dgm RCSB], [https://www.ebi.ac.uk/pdbsum/2dgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dgm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DCEB_ECOLI DCEB_ECOLI]
== 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/dg/2dgm_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/main_output.php?pdb_ID=2dgm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Escherichia coli and other enterobacteria exploit the H+ -consuming reaction catalysed by glutamate decarboxylase to survive the stomach acidity before reaching the intestine. Here we show that chloride, extremely abundant in gastric secretions, is an allosteric activator producing a 10-fold increase in the decarboxylase activity at pH 5.6. Cooperativity and sensitivity to chloride were lost when the N-terminal 14 residues, involved in the formation of two triple-helix bundles, were deleted by mutagenesis. X-ray structures, obtained in the presence of the substrate analogue acetate, identified halide-binding sites at the base of each N-terminal helix, showed how halide binding is responsible for bundle stability and demonstrated that the interconversion between active and inactive forms of the enzyme is a stepwise process. We also discovered an entirely novel structure of the cofactor pyridoxal 5'-phosphate (aldamine) to be responsible for the reversibly inactivated enzyme. Our results link the entry of chloride ions, via the H+/Cl- exchange activities of ClC-ec1, to the trigger of the acid stress response in the cell when the intracellular proton concentration has not yet reached fatal values.


===Crystal structure of Escherichia coli GadB in complex with iodide===
Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB.,Gut H, Pennacchietti E, John RA, Bossa F, Capitani G, De Biase D, Grutter MG EMBO J. 2006 Jun 7;25(11):2643-51. Epub 2006 May 4. PMID:16675957<ref>PMID:16675957</ref>


{{ABSTRACT_PUBMED_16675957}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2dgm" style="background-color:#fffaf0;"></div>
[[2dgm]] is a 6 chain structure with 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=2DGM OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:016675957</ref><ref group="xtra">PMID:012912902</ref><references group="xtra"/>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamate decarboxylase]]
[[Category: Large Structures]]
[[Category: Capitani, G.]]
[[Category: Capitani G]]
[[Category: Gruetter, M G.]]
[[Category: Gruetter MG]]
[[Category: Gut, H.]]
[[Category: Gut H]]
[[Category: Gadb complexed with iodide]]
[[Category: Lyase]]