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2dgk

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{{STRUCTURE_2dgk| PDB=2dgk | SCENE= }}
{{STRUCTURE_2dgk| PDB=2dgk | SCENE= }}
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'''Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine)'''
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===Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine)===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16675957}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16675957 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16675957}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16675957 16675957]
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]
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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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamate decarboxylase]]
[[Category: Glutamate decarboxylase]]
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[[Category: Gadbd1-14]]
[[Category: Gadbd1-14]]
[[Category: Substituted aldamine]]
[[Category: Substituted aldamine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:22:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:14:45 2008''

Revision as of 15:14, 27 July 2008

Image:2dgk.png

Template:STRUCTURE 2dgk

Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine)

Template:ABSTRACT PUBMED 16675957

About this Structure

2DGK 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

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:12912902

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