2VYC: Crystal Structure Of Acid Induced Arginine Decarboxylase From E. Coli

Citation:
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.
PDB ID: 2VYCDownload
MMDB ID: 70510
PDB Deposition Date: 2008/7/22
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 2VYC: decameric; determined by author and by software (PISA)
Molecular Components in 2VYC
Label Count Molecule
Proteins (15 molecules)
15
Biodegradative Arginine Decarboxylase(Gene symbol: adiA)
Molecule annotation
Chemicals (10 molecules)
1
10
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.