Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase.
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.
Cordeiro
Artur T
AT
Laboratório de Cristalografia de Proteínas, Departamento de Física e Química, Faculdade de Ciências Farmacêuticas de Ribeirão Preto-USP, Ribeirão Preto, SP 14040-903, Brazil.
Feliciano
Patricia R
PR
Nonato
M Cristina
MC
D000818:Animals; D003460:Crystallization; D000090722:Dihydroorotate Dehydrogenase; D018320:Leishmania major / Q000201:enzymology*; D018020:Lithium Compounds / Q000378:metabolism; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry* / Q000302:isolation & purification; D013431:Sulfates / Q000378:metabolism; D014961:X-Ray Diffraction
D000090722:Dihydroorotate Dehydrogenase; D018020:Lithium Compounds; D013431:Sulfates; C054097:lithium sulfate; D044925:Oxidoreductases Acting on CH-CH Group Donors