› 2rg1

X-ray diffraction
1.85Å resolution

Crystal structure of E. coli WrbA apoprotein

Released:
DOI: 10.2210/pdb2rg1/pdb
PDB entry 2rg1 coloured by chain, front view.
PDB entry 2rg1 coloured by chain, side view.
PDB entry 2rg1 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural organization of WrbA in apo- and holoprotein crystals.
Wolfova J, Smatanova IK, Brynda J, Mesters JR, Lapkouski M, Kuty M, Natalello A, Chatterjee N, Chern SY, Ebbel E, Ricci A, Grandori R, Ettrich R, Carey J
Biochim Biophys Acta 1794 1288-98 (2009)
PMID: 19665595

Function and Biology Details

Reaction catalysed: 
NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)H dehydrogenase (quinone) Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 20.86 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A8G6 (Residues: 1-198; Coverage: 100%)
Gene names: JW0989, b1004, wrbA
Sequence domains: NADPH-dependent FMN reductase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P21212
Unit cell:
a: 70.85Å b: 75.69Å c: 56.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.195
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Cofactor binding protects flavodoxin against oxidative stress.
Lindhoud et al. (2012)
4 more

2 mentions without citation

Biphasic kinetic behavior of E. coli WrbA, an FMN-dependent NAD(P)H:quinone oxidoreductase.
Kishko et al. (2012)
1 more