Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla

Abstract

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.