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

Research output: Contribution to journalArticle

29 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)198-205
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume338
Issue number1
DOIs
StatePublished - Dec 9 2005

Fingerprint

Catechol 1,2-Dioxygenase
Pseudomonas
Dimerization
Lipids
Isoenzymes
Binding Sites
Dioxygenases
Sulfhydryl Reagents
Fasteners
Plastics
Catalytic Domain
Carrier Proteins
Monomers
Crystal structure
Peptides

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Earhart, C. A., Vetting, M. W., Gosu, R., Michaud-Soret, I., Que, L., & Ohlendorf, D. H. (2005). Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla. Biochemical and Biophysical Research Communications, 338(1), 198-205. https://doi.org/10.1016/j.bbrc.2005.08.221

Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla. / Earhart, Cathleen A.; Vetting, Matthew W.; Gosu, Ramachandraiah; Michaud-Soret, Isabelle; Que, Lawrence; Ohlendorf, Douglas H.

In: Biochemical and Biophysical Research Communications, Vol. 338, No. 1, 09.12.2005, p. 198-205.

Research output: Contribution to journalArticle

Earhart, CA, Vetting, MW, Gosu, R, Michaud-Soret, I, Que, L & Ohlendorf, DH 2005, 'Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla', Biochemical and Biophysical Research Communications, vol. 338, no. 1, pp. 198-205. https://doi.org/10.1016/j.bbrc.2005.08.221
Earhart, Cathleen A. ; Vetting, Matthew W. ; Gosu, Ramachandraiah ; Michaud-Soret, Isabelle ; Que, Lawrence ; Ohlendorf, Douglas H. / Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla. In: Biochemical and Biophysical Research Communications. 2005 ; Vol. 338, No. 1. pp. 198-205.
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