Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1.
The metalloenzyme catechol 1,2-dioxygenase from Pseudomonas arvilla C-1 consists of three isozymes formed by combinations of two non-identical subunits; alpha alpha, alpha beta and beta beta; with molecular masses of 59,000, 63,000 and 67,000 Da, respectively. The alpha alpha isozyme crystallizes in the orthorhombic space group C222(1) with unit cell dimensions a = 62.7 A, b = 71.5 A, c = 187.1 A. The rectangular plates diffract to 2.6 A 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.
Earhart
C A
CA
Department of Biochemistry, University of Minnesota Medical School, Minneapolis 55455.
Hall
M D
MD
Michaud-Soret
I
I
Que
L
L
Ohlendorf
D H
DH
D050548:Catechol 1,2-Dioxygenase; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D049308:Dioxygenases; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D010105:Oxygenases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*
D007527:Isoenzymes; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase