التفاصيل البيبلوغرافية
| العنوان: |
Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major. |
| المؤلفون: |
Faim, Lívia Maria, e Silva, Ivan Rosa, Dias, Marcio Vinicius Bertacine, Pereira, Humberto D'Muniz, Brandao-Neto, José, da Silva, Marco Túlio Alves, Thiemann, Otavio Henrique |
| المصدر: |
Acta Crystallographica: Section F (Wiley-Blackwell); Aug2013, Vol. 69 Issue 8, p864-867, 4p |
| مصطلحات موضوعية: |
SELENIUM, ADENOSINE triphosphatase, SELENOCYSTEINE, PROTEOLYSIS, TRYPANOSOMA brucei |
| مستخلص: |
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. [ABSTRACT FROM AUTHOR] |
|
Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Complementary Index |
Full Text Finder