- Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase.
Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase.
Acta crystallographica. Section F, Structural biology and crystallization communications (2006-10-03)
Artur T Cordeiro, Patricia R Feliciano, M Cristina Nonato
PMID17012810
RÉSUMÉ
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.