› 1dj7

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF FERREDOXIN THIOREDOXIN REDUCTASE

Released:
DOI: 10.2210/pdb1dj7/pdb
PDB entry 1dj7 coloured by chain, front view.
PDB entry 1dj7 coloured by chain, side view.
PDB entry 1dj7 coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803
Primary publication:
Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.
Dai S, Schwendtmayer C, Sch��rmann P, Ramaswamy S, Eklund H
Science 287 655-8 (2000)
PMID: 10649999

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176276 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ferredoxin-thioredoxin reductase, catalytic chain Chain: A
Molecule details ›
Chain: A
Length: 117 amino acids
Theoretical weight: 13.27 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli
UniProt:
  • Canonical: Q55389 (Residues: 2-118; Coverage: 99%)
Gene names: ftrC, sll0554
Sequence domains: Ferredoxin thioredoxin reductase catalytic beta chain
Structure domains: Ferredoxin thioredoxin reductase catalytic beta subunit
Ferredoxin-thioredoxin reductase, variable chain Chain: B
Molecule details ›
Chain: B
Length: 75 amino acids
Theoretical weight: 8.57 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli
UniProt:
  • Canonical: Q55781 (Residues: 1-75; Coverage: 100%)
Gene names: ftrV, ssr0330
Sequence domains: Ferredoxin thioredoxin reductase variable alpha chain
Structure domains: SH3 type barrels.

Ligands and Environments

2 bound ligands:
Ligand SF4 1 x SF4
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P43212
Unit cell:
a: 45.296Å b: 45.296Å c: 172.147Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.264 0.238 0.278
Expression system: Escherichia coli

Quick links

Citations

35 review citations

Physiological functions of thioredoxin and thioredoxin reductase.
Arnér et al. (2000)
34 more

11 mentions without citation

Coevolution at protein complex interfaces can be detected by the complementarity trace with important impact for predictive docking.
Madaoui et al. (2008)
10 more