title: Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major.
abstract: Selenophosphate synthetase (SPS) plays an indispensable role in selenium metabolism, being responsible for catalyzing the activation of selenide with adenosine 5'-triphosphate (ATP) to generate selenophosphate, the essential selenium donor for selenocysteine synthesis. Recombinant full-length Leishmania major SPS (LmSPS2) was recalcitrant to crystallization. Therefore, a limited proteolysis technique was used and a stable N-terminal truncated construct (ΔN-LmSPS2) yielded suitable crystals. The Trypanosoma brucei SPS orthologue (TbSPS2) was crystallized by the microbatch method using paraffin oil. X-ray diffraction data were collected to resolutions of 1.9 Å for ΔN-LmSPS2 and 3.4 Å for TbSPS2.
authors.affiliation: Institute of Physics, University of São Paulo, Avenida Trabalhador São-carlense 400, 13566-590 São Carlos-SP, Brazil.
authors.forename: Lívia Maria
authors.initials: LM
authors.lastname: Faim
authors.forename: Ivan
authors.initials: I
authors.lastname: Rosa e Silva
authors.forename: Marcio Vinicius
authors.initials: MV
authors.lastname: Bertacine Dias
authors.forename: Humberto
authors.initials: H
authors.lastname: D'Muniz Pereira
authors.forename: José
authors.initials: J
authors.lastname: Brandao-Neto
authors.forename: Marco Túlio
authors.initials: MT
authors.lastname: Alves da Silva
authors.forename: Otavio Henrique
authors.initials: OH
authors.lastname: Thiemann
mesh_terms: D003460:Crystallization; D018320:Leishmania major; D010770:Phosphotransferases / Q000737:chemistry*; D015800:Protozoan Proteins / Q000737:chemistry*; D014346:Trypanosoma brucei brucei; D014961:X-Ray Diffraction
chemical_list: D015800:Protozoan Proteins; D010770:Phosphotransferases; C499551:Sephs2 protein, mouse; C062762:selenophosphate synthetase
keywords: Leishmania major; Trypanosoma brucei; selenocysteine; selenophosphate synthetase
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