2dgl: Difference between revisions

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New page: left|200px<br /><applet load="2dgl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dgl, resolution 3.15Å" /> '''Crystal structure of...
 
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[[Image:2dgl.gif|left|200px]]<br /><applet load="2dgl" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2dgl.gif|left|200px]]<br /><applet load="2dgl" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2dgl, resolution 3.15&Aring;" />
caption="2dgl, resolution 3.15&Aring;" />
'''Crystal structure of Escherichia coli GadB in complex with bromide'''<br />
'''Crystal structure of Escherichia coli GadB in complex with bromide'''<br />


==Overview==
==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.
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==
==About this Structure==
2DGL 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 BR, PLP and ACY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DGL OCA].  
2DGL 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=BR:'>BR</scene>, <scene name='pdbligand=PLP:'>PLP</scene> and <scene name='pdbligand=ACY:'>ACY</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=2DGL OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Capitani, G.]]
[[Category: Capitani, G.]]
[[Category: Gruetter, M.G.]]
[[Category: Gruetter, M G.]]
[[Category: Gut, H.]]
[[Category: Gut, H.]]
[[Category: ACY]]
[[Category: ACY]]
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[[Category: gadb complexed with bromide]]
[[Category: gadb complexed with bromide]]


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