Expression, purification and crystallization of the cofactor-independent monooxygenase SnoaB from the nogalamycin biosynthetic pathway

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):256-9. doi: 10.1107/S1744309109001389. Epub 2009 Feb 14.

Abstract

12-deoxy-nogalonic acid oxygenase (SnoaB) catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to yield nogalonic acid, which is one of the steps in the biosynthesis of the polyketide nogalamycin in Streptomyces nogalater. SnoaB belongs to a family of small cofactor-free oxygenases which carry out oxygenation reactions without the aid of any prosthetic group, cofactor or metal ion. Recombinant SnoaB was crystallized in space group P2(1)2(1)2, with unit-cell parameters a = 58.8, b = 114.1, c = 49.5 A, and these crystals diffracted to 2.4 A resolution. Recombinant SnoaB does not contain any methionine residues and three double mutants were designed and produced for the preparation of selenomethionine-substituted samples. The selenomethionine-substituted mutant F40M/L89M crystallized in the same space group as the native enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Catalysis
  • Coenzymes / metabolism*
  • Crystallization
  • Crystallography, X-Ray
  • Mixed Function Oxygenases / chemistry
  • Mixed Function Oxygenases / isolation & purification*
  • Mixed Function Oxygenases / metabolism*
  • Molecular Sequence Data
  • Mutant Proteins / chemistry
  • Mutant Proteins / metabolism
  • Nogalamycin / biosynthesis*
  • Nogalamycin / chemistry
  • Selenomethionine / metabolism
  • Sequence Alignment
  • Streptomyces / enzymology*

Substances

  • Coenzymes
  • Mutant Proteins
  • Selenomethionine
  • Mixed Function Oxygenases
  • Nogalamycin