Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1

Cathleen A. Earhart, Michael D. Hall, Isabelle Michaud-Soret, Lawrence Que, Douglas H. Ohlendorf

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

The metalloenzyme catechol 1,2-dioxygenase from Pseudomonas arvilla C-1 consists of three isozymes formed by combinations of two non-identical subunits; αα, αβ and ββ; with molecular masses of 59,000, 63,000 and 67,000 Da, respectively. The αα isozyme crystallizes in the orthorhombic space group C2221 with unit cell dimensions a = 62.7 Å, b = 71.5 Å, c = 187.1 Å. The rectangular plates diffract to 2.6 Å resolution. This is the first dioxygenase to be crystallized that uses catechol as a substrate. Comparison of the structure of this enzyme with protocatechuate 3,4-dioxygenase will provide basic information about the mechanisms of subunit association, substrate selectivity, and the origins of metabolic diversity in enzymes.

Original languageEnglish (US)
Pages (from-to)377-378
Number of pages2
JournalJournal of Molecular Biology
Volume236
Issue number1
DOIs
StatePublished - Feb 10 1994

Keywords

  • Crystallization
  • Dioxygenases
  • Evolution
  • Pseudomonas arvilla
  • X-ray crystallography

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