› 1mpy

X-ray diffraction
2.8Å resolution

STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2

Released:
DOI: 10.2210/pdb1mpy/pdb
PDB entry 1mpy coloured by chain, front view.
PDB entry 1mpy coloured by chain, side view.
PDB entry 1mpy coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2.
Kita A, Kita S, Fujisawa I, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K
Structure 7 25-34 (1999)
PMID: 10368270

Function and Biology Details

Reaction catalysed: 
Catechol + O(2) = 2-hydroxymuconate-6-semialdehyde
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139106 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metapyrocatechase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 307 amino acids
Theoretical weight: 35.2 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli str. K-12 substr. W3110
UniProt:
  • Canonical: P06622 (Residues: 1-307; Coverage: 100%)
Gene name: xylE
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

2 bound ligands:
Ligand FE2 4 x FE2
Ligand ACN 4 x ACN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P42212
Unit cell:
a: 264Å b: 264Å c: 59.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.28
Expression system: Escherichia coli str. K-12 substr. W3110

Quick links

Citations

9 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
8 more

15 mentions without citation

Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases.
Vetting et al. (2004)
14 more