Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla

Cathleen A. Earhart, Matthew W. Vetting, Ramachandraiah Gosu, Isabelle Michaud-Soret, Lawrence Que, Douglas H. Ohlendorf

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34 Scopus citations


Catechol 1,2-dioxygenase was first studied by Hayaishi and colleagues in 1950. In 1967, catechol 1,2-dioxygenase from Pseudomonas arvilla C-1 (PaCTD) was chosen as a model system for the catecholic intradiol dioxygenases due to its activity, stability and expression level. Here we report the 2.65 Å structure of the ββ isozyme of PaCTD. The structure supports the hypothesis first made by Vetting and Ohlendorf [The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker, Struct. Fold. Des. 8 (2000) 429-440.] that the catechol 1,2-dioxygenases are lipid binding proteins. The 5 amino-terminal helices involved in dimerization and forming the lipid binding site are shown to be plastic in their positions and orientations. The sequence differences between the α and β polypeptides are located at the part of the monomers distant from dimerization surface and thus permit the formation of the 3 isozymes (αα, αβ, and ββ) of PaCTD. The reported inactivation by sulfhydryl-modifying reagents is explained by the structure. The 10-residue Helix F (residues 203-212) is proposed to be central in communicating between the lipid binding site and the active site.

Original languageEnglish (US)
Pages (from-to)198-205
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Dec 9 2005
Externally publishedYes


  • Intradiol dioxygenase
  • Lipid binding protein
  • Metalloenzyme
  • Nonheme iron
  • X-ray crystallography

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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