1PMO

Crystal structure of Escherichia coli GadB (neutral pH)

1PMO の概要

• エントリーDOI: 10.2210/pdb1pmo/pdb
• 関連するPDBエントリー: 1PMM
• 分子名称: Glutamate decarboxylase beta, (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: neutral-ph form of gadb, lyase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P69910
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 319965.26

構造登録者

Capitani, G.,De Biase, D.,Aurizi, C.,Gut, H.,Bossa, F.,Grutter, M.G. (登録日: 2003-06-11, 公開日: 2004-02-17, 最終更新日: 2024-02-14)

主引用文献

Capitani, G.,De Biase, D.,Aurizi, C.,Gut, H.,Bossa, F.,Grutter, M.G.
Crystal structure and functional analysis of escherichia coli glutamate decarboxylase
Embo J., 22:4027-4037, 2003

PubMed Abstract: 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.

PubMed: 12912902
DOI: 10.1093/emboj/cdg403

実験手法

X-RAY DIFFRACTION (2.3 Å)