› 2vyc

X-ray diffraction
2.4Å resolution

Crystal Structure of Acid Induced Arginine Decarboxylase from E. coli

Released:
DOI: 10.2210/pdb2vyc/pdb
PDB entry 2vyc coloured by chain, front view.
PDB entry 2vyc coloured by chain, side view.
PDB entry 2vyc coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: reversible decamer assembly controls enzyme activity.
Andréll J, Hicks MG, Palmer T, Carpenter EP, Iwata S, Maher MJ
Biochemistry 48 3915-27 (2009)
PMID: 19298070

Function and Biology Details

Reaction catalysed: 
L-arginine = agmatine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151253 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biodegradative arginine decarboxylase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 755 amino acids
Theoretical weight: 84.51 KDa
Source organism: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28629 (Residues: 1-755; Coverage: 100%)
Gene names: JW5731, adi, adiA, b4117
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 10 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4, ESRF BEAMLINE ID14-3
Spacegroup: P64
Unit cell:
a: 197.651Å b: 197.651Å c: 450.322Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.229

Quick links

Citations

8 review citations

Mechanisms of acid resistance in Escherichia coli.
Kanjee et al. (2013)
7 more

8 mentions without citation

Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase.
Kanjee et al. (2011)
7 more