› 5ygq

X-ray diffraction
2.4Å resolution

Crystal Structure of Ferredoxin NADP+ Oxidoreductase from Rhodopseudomonas palustris

Released:
DOI: 10.2210/pdb5ygq/pdb
PDB entry 5ygq coloured by chain, front view.
PDB entry 5ygq coloured by chain, side view.
PDB entry 5ygq coloured by chain, top view.
Source organism: Rhodopseudomonas palustris CGA009
Primary publication:
Kinetic and structural insight into a role of the re-face Tyr328 residue of the homodimer type ferredoxin-NADP+ oxidoreductase from Rhodopseudomonas palustris in the reaction with NADP+/NADPH.
Seo D, Muraki N, Kurisu G
Biochim Biophys Acta Bioenerg 1861 148140 (2020)
PMID: 31838096

Function and Biology Details

Reaction catalysed: 
2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin--NADP reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 342 amino acids
Theoretical weight: 37.06 KDa
Source organism: Rhodopseudomonas palustris CGA009
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6N2U4 (Residues: 1-342; Coverage: 100%)
Gene name: RPA3954
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 70.868Å b: 81.227Å c: 122.182Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.218 0.263
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

The Role of the si-Face Tyrosine of a Homodimeric Ferredoxin-NADP+ Oxidoreductase from Bacillus subtilis during Complex Formation and Redox Equivalent Transfer with NADP+/H and Ferredoxin.
Seo D. (2023)

3 mentions without citation

Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries.
Minjárez-Sáenz et al. (2022)
2 more