› 2puk

X-ray diffraction
3Å resolution

Crystal structure of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin m

Released:
DOI: 10.2210/pdb2puk/pdb
PDB entry 2puk coloured by chain, front view.
PDB entry 2puk coloured by chain, side view.
PDB entry 2puk coloured by chain, top view.
Source organisms:
Primary publication:
Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase.
Dai S, Friemann R, Glauser DA, Bourquin F, Manieri W, Schürmann P, Eklund H
Nature 448 92-6 (2007)
PMID: 17611542

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 trimer (preferred)
PDBe Complex ID:
PDB-CPX-139649 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ferredoxin-thioredoxin reductase, catalytic chain Chains: A, E
Molecule details ›
Chains: A, E
Length: 109 amino acids
Theoretical weight: 12.45 KDa
Source organism: Synechocystis sp.
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q55389 (Residues: 9-116; Coverage: 92%)
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 Chains: B, F
Molecule details ›
Chains: B, F
Length: 73 amino acids
Theoretical weight: 8.33 KDa
Source organism: Synechocystis sp.
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q55781 (Residues: 1-73; Coverage: 97%)
Gene names: ftrV, ssr0330
Sequence domains: Ferredoxin thioredoxin reductase variable alpha chain
Structure domains: SH3 type barrels.
Thioredoxin M-type Md Chains: C, G
Molecule details ›
Chains: C, G
Length: 106 amino acids
Theoretical weight: 11.86 KDa
Source organism: Spinacia oleracea
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P07591 (Residues: 75-180; Coverage: 59%)
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand SF4 2 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 53.952Å b: 42.223Å c: 145.344Å
α: 90° β: 90.29° γ: 90°
R-values:
R R work R free
0.237 0.235 0.284
Expression system: Escherichia coli BL21

Quick links

Citations

15 review citations

Physiological functions of mineral micronutrients (Cu, Zn, Mn, Fe, Ni, Mo, B, Cl).
Hänsch et al. (2009)
14 more

6 mentions without citation

Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1.
Ma et al. (2011)
5 more