1pmo

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1pmo, resolution 2.30Å ()
Ligands: ,
Gene: GADB (Escherichia coli)
Activity: Glutamate decarboxylase, with EC number 4.1.1.15
Related: 1pmm
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Escherichia coli GadB (neutral pH)

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1pmo is a 6 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Capitani G, De Biase D, Aurizi C, Gut H, Bossa F, Grutter MG. Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase. EMBO J. 2003 Aug 15;22(16):4027-37. PMID:12912902 doi:http://dx.doi.org/10.1093/emboj/cdg403

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