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Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase.

ABSTRACT: Dihydroorotate dehydrogenases (DHODHs) are flavin-containing enzymes that catalyze the oxidation of L-dihydroorotate to orotate, the fourth step in the de novo pyrimidine nucleotide synthesis pathway. In this study, DHODH from Leishmania major has been crystallized by the vapour-diffusion technique using lithium sulfate as the precipitating agent. The crystals belong to space group P6(1), with unit-cell parameters a = 143.7, c = 69.8 A. X-ray diffraction data were collected to 2.0 A resolution using an in-house rotating-anode generator. Analysis of the solvent content and the self-rotation function indicate the presence of two molecules in the asymmetric unit. The structure has been solved by the molecular-replacement technique.

SUBMITTER: Cordeiro AT

PROVIDER: S-EPMC2225193 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase.

Cordeiro Artur T AT Feliciano Patricia R PR Nonato M Cristina MC

Acta crystallographica. Section F, Structural biology and crystallization communications 20060930 Pt 10

Dihydroorotate dehydrogenases (DHODHs) are flavin-containing enzymes that catalyze the oxidation of L-dihydroorotate to orotate, the fourth step in the de novo pyrimidine nucleotide synthesis pathway. In this study, DHODH from Leishmania major has been crystallized by the vapour-diffusion technique using lithium sulfate as the precipitating agent. The crystals belong to space group P6(1), with unit-cell parameters a = 143.7, c = 69.8 A. X-ray diffraction data were collected to 2.0 A resolution u ...[more]

PMID: 17012810

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