A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Expression, purification and crystallization of the cofactor-independent monooxygenase SnoaB from the nogalamycin biosynthetic pathway
Tekijät: Koskiniemi H, Grocholski T, Schneider G, Niemi J
Kustantaja: WILEY-BLACKWELL PUBLISHING, INC
Julkaisuvuosi: 2009
Lehti:: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Tietokannassa oleva lehden nimi: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Lehden akronyymi: ACTA CRYSTALLOGR F
Vuosikerta: 65
Aloitussivu: 256
Lopetussivu: 259
Sivujen määrä: 4
ISSN: 1744-3091
DOI: https://doi.org/10.1107/S1744309109001389
Tiivistelmä
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 angstrom, and these crystals diffracted to 2.4 angstrom 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.
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 angstrom, and these crystals diffracted to 2.4 angstrom 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.
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