| Autor: |
de Oliveira, Marcos Antonio, Genu, Victor, Discola, Karen Fulan, Alves, Simone Vidigal, Netto, Luis Eduardo Soares, Guimarães, Beatriz Gomes |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section F (Wiley-Blackwell); Aug2007, Vol. 63 Issue 8, p665-668, 4p, 3 Diagrams, 1 Chart |
| Abstrakt: |
Saccharomyces cerevisiae cytosolic thioredoxin peroxidase 1 (cTPxI or Tsa1) is a bifunctional enzyme with protective roles in cellular defence against oxidative and thermal stress that exhibits both peroxidase and chaperone activities. Protein overoxidation and/or high temperatures induce great changes in its quaternary structure and lead to its assembly into large complexes that possess chaperone activity. A recombinant mutant of Tsa1 from S. cerevisiae, with Cys47 substituted by serine, was overexpressed in Escherichia coli as a His6-tagged fusion protein and purified by nickel-affinity chromatography. Crystals were obtained from protein previously treated with 1,4-dithiothreitol by the hanging-drop vapour-diffusion method using PEG 3000 as precipitant and sodium fluoride as an additive. Diffraction data were collected to 2.8 Å resolution using a synchrotron-radiation source. The crystal structure was solved by molecular-replacement methods and structure refinement is currently in progress. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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