2dgm

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[[Image:2dgm.gif|left|200px]]<br /><applet load="2dgm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2dgm.gif|left|200px]]
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caption="2dgm, resolution 1.95&Aring;" />
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'''Crystal structure of Escherichia coli GadB in complex with iodide'''<br />
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{{Structure
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|PDB= 2dgm |SIZE=350|CAPTION= <scene name='initialview01'>2dgm</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
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|ACTIVITY= [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]
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|GENE= gadB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of Escherichia coli GadB in complex with iodide'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2DGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=IOD:'>IOD</scene>, <scene name='pdbligand=PLP:'>PLP</scene>, <scene name='pdbligand=FMT:'>FMT</scene>, <scene name='pdbligand=ACY:'>ACY</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DGM OCA].
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2DGM 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=2DGM OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16675957 16675957]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16675957 16675957]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamate decarboxylase]]
[[Category: Glutamate decarboxylase]]
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[[Category: gadb complexed with iodide]]
[[Category: gadb complexed with iodide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:26:58 2008''

Revision as of 14:27, 20 March 2008


PDB ID 2dgm

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: , , , and
Gene: gadB (Escherichia coli)
Activity: Glutamate decarboxylase, with EC number 4.1.1.15
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Escherichia coli GadB in complex with iodide


Overview

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.

About this Structure

2DGM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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