› 3klj

X-ray diffraction
2.1Å resolution

Crystal structure of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum

Released:
DOI: 10.2210/pdb3klj/pdb
PDB entry 3klj coloured by chain, front view.
PDB entry 3klj coloured by chain, side view.
PDB entry 3klj coloured by chain, top view.
Source organism: Clostridium acetobutylicum
Primary publication:
Crystal structure of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum: a key component of the dioxygen scavenging system in obligatory anaerobes.
Nishikawa K, Shomura Y, Kawasaki S, Niimura Y, Higuchi Y
Proteins 78 1066-70 (2010)
PMID: 20017214

Function and Biology Details

Reaction catalysed: 
2 reduced rubredoxin + NAD(+) + H(+) = 2 oxidized rubredoxin + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189574 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH-rubredoxin oxidoreductase Chain: A
Molecule details ›
Chain: A
Length: 385 amino acids
Theoretical weight: 42.17 KDa
Source organism: Clostridium acetobutylicum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9AL95 (Residues: 2-379; Coverage: 100%)
Gene names: CA_C2448, nroR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P4322
Unit cell:
a: 98.576Å b: 98.576Å c: 88.267Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.254
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

A natural fusion of flavodiiron, rubredoxin, and rubredoxin oxidoreductase domains is a self-sufficient water-forming oxidase of Trichomonas vaginalis.
Abdulaziz et al. (2022)
3 more

2 mentions without citation

TNF superfamily protein-protein interactions: feasibility of small- molecule modulation.
Song et al. (2015)
1 more