2VYC

Crystal Structure of Acid Induced Arginine Decarboxylase from E. coli

2VYC の概要

• エントリーDOI: 10.2210/pdb2vyc/pdb
• 分子名称: BIODEGRADATIVE ARGININE DECARBOXYLASE, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: arginine decarboxylase, pyridoxal phosphate, plp-dependent enzyme, lyase, decarboxylase, acid resistance
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cytoplasm: P28629
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 847592.04

構造登録者

Andrell, J.,Hicks, M.G.,Palmer, T.,Carpenter, E.P.,Iwata, S.,Maher, M.J. (登録日: 2008-07-22, 公開日: 2009-03-31, 最終更新日: 2025-04-09)

主引用文献

Andrell, J.,Hicks, M.G.,Palmer, T.,Carpenter, E.P.,Iwata, S.,Maher, M.J.
Crystal Structure of the Acid Induced Arginine Decarboxylase from Escherichia Coli: Reversible Decamer Assembly Controls Enzyme Activity.
Biochemistry, 48:3915-, 2009

PubMed Abstract: The acid-induced arginine decarboxylase is part of an enzymatic system in Escherichia coli that contributes to making this organism acid resistant. The arginine decarboxylase is a vitamin B(6)-dependent enzyme that is active at acidic pH. It consumes a proton in the decarboxylation of arginine to agmatine, and by working in tandem with an arginine-agmatine antiporter, this enzymatic cycle protects the organism by preventing the accumulation of protons inside the cell. We have determined the structure of the acid-induced arginine decarboxylase by X-ray crystallography to 2.4 A resolution. The arginine decarboxylase structure revealed a ca. 800 kDa decamer composed as a pentamer of five homodimers. Each homodimer has an abundance of acidic surface residues, which at neutral pH prevents inactive homodimers from associating into active decamers. Conversely, acidic conditions favor the assembly of active decamers. Therefore, the structure of arginine decarboxylase presents a mechanism by which its activity is modulated by external pH.

PubMed: 19298070
DOI: 10.1021/BI900075D

実験手法

X-RAY DIFFRACTION (2.4 Å)