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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

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Autor(es):
Faim, Livia Maria [1] ; Rosa e Silva, Ivan [1] ; Bertacine Dias, Marcio Vinicius [2, 3] ; Pereira, Humberto D'Muniz [1] ; Brandao-Neto, Jose [4] ; Alves da Silva, Marco Tulio [1] ; Thiemann, Otavio Henrique [1]
Número total de Autores: 7
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Inst Phys, BR-13566590 Sao Carlos, SP - Brazil
[2] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA - England
[3] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Biosci Natl Lab LNBio, BR-13083970 Campinas, SP - Brazil
[4] Diamond Light Source, Didcot OX11 0DE, Oxon - England
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Fonte: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS; v. 69, n. 8, p. 864-867, AUG 2013.
Citações Web of Science: 1
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
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs