› 3nl1

X-ray diffraction
2.16Å resolution

Crystal Structure of Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans Adducts with gentisate

Released:
DOI: 10.2210/pdb3nl1/pdb
PDB entry 3nl1 coloured by chain, front view.
PDB entry 3nl1 coloured by chain, side view.
PDB entry 3nl1 coloured by chain, top view.
Source organism: Pseudaminobacter salicylatoxidans
Primary publication:
Crystal structures of salicylate 1,2-dioxygenase-substrates adducts: A step towards the comprehension of the structural basis for substrate selection in class III ring cleaving dioxygenases.
Ferraroni M, Matera I, Steimer L, Bürger S, Scozzafava A, Stolz A, Briganti F
J Struct Biol 177 431-8 (2012)
PMID: 22155290

Function and Biology Details

Reaction catalysed: 
2,5-dihydroxybenzoate + O(2) = maleylpyruvate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179305 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cupin type-2 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 368 amino acids
Theoretical weight: 41.14 KDa
Source organism: Pseudaminobacter salicylatoxidans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q67FT0 (Residues: 1-368; Coverage: 100%)
Gene name: C7441_11945
Sequence domains: Cupin domain
Structure domains: Jelly Rolls

Ligands and Environments

3 bound ligands:
Ligand FE2 1 x FE2
Ligand GTQ 1 x GTQ
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: I222
Unit cell:
a: 76.58Å b: 86.97Å c: 166.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.161 0.212
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Ring-cleaving dioxygenases with a cupin fold.
Fetzner S. (2012)
9 other articles

7 mentions without citation

Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers.
Buongiorno et al. (2013)
6 more