› 2ohi

X-ray diffraction
2.3Å resolution

Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, reduced state

Released:
DOI: 10.2210/pdb2ohi/pdb
PDB entry 2ohi coloured by chain, front view.
PDB entry 2ohi coloured by chain, side view.
PDB entry 2ohi coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O.
Seedorf H, Hagemeier CH, Shima S, Thauer RK, Warkentin E, Ermler U
FEBS J 274 1588-99 (2007)
PMID: 17480207

Function and Biology Details

Reaction catalysed: 
2 reduced coenzyme F420 + O(2) = 2 oxidized coenzyme F420 + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-175875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coenzyme F420H(2) oxidase Chains: A, B, D, E, G, H, I, J
Molecule details ›
Chains: A, B, D, E, G, H, I, J
Length: 404 amino acids
Theoretical weight: 45.26 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q50497 (Residues: 1-404; Coverage: 100%)
Gene names: MTBMA_c17400, fpaA, fprA, fprA3
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FMN 8 x FMN
2 bound ligands:
Ligand FE 16 x FE
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 97.798Å b: 123.113Å c: 135.864Å
α: 90° β: 103.4° γ: 90°
R-values:
R R work R free
0.206 0.203 0.269
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Cyanobacterial Oxygenic Photosynthesis is Protected by Flavodiiron Proteins.
Allahverdiyeva et al. (2015)
7 more

3 mentions without citation

Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.
Greening et al. (2016)
2 more