| Texto completo | |
| Autor(es): |
Faim, Livia Maria
;
Rosa e Silva, Ivan
;
Bertacine Dias, Marcio Vinicius
;
Pereira, Humberto D'Muniz
;
Brandao-Neto, Jose
;
Alves da Silva, Marco Tulio
;
Thiemann, Otavio Henrique
Número total de Autores: 7
|
| Tipo de documento: | Artigo Científico |
| Fonte: | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS; v. 69, p. 4-pg., 2013-08-01. |
| Resumo | |
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 (Delta 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 angstrom for Delta N-LmSPS2 and 3.4 angstrom for TbSPS2. (AU) | |
| Processo FAPESP: | 98/14138-2 - Center for Structural Molecular Biotechnology |
| Beneficiário: | Glaucius Oliva |
| Modalidade de apoio: | Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs |