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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 (?N-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 ?N-LmSPS2 and 3.4 Å for TbSPS2.

SUBMITTER: Faim LM 

PROVIDER: S-EPMC3729160 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major.

Faim Lívia Maria LM   Rosa e Silva Ivan I   Bertacine Dias Marcio Vinicius MV   D'Muniz Pereira Humberto H   Brandao-Neto José J   Alves da Silva Marco Túlio MT   Thiemann Otavio Henrique OH  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130727 Pt 8

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  ...[more]

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