Crystallization and preliminary X-ray diffraction analysis of NADPH-dependent thioredoxin reductase I from Saccharomyces cerevisiae

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Marcos Antonio de OliveiraBeatriz Gomes Guimarães

Abstract

Thioredoxin reductase 1 (Trr1) from Saccharomyces cerevisiae is a member of the family of pyridine nucleotide-disulfide oxidoreductases capable of reducing the redox-active disulfide bond of the cytosolic thioredoxin 1 (Trx1) and thioredoxin 2 (Trx2). NADPH, Trr1 and Trx1 (or Trx2) comprise the thioredoxin system, which is involved in several biological processes, including the reduction of disulfide bonds and response to oxidative stress. Recombinant Trr1 was expressed in Escherichia coli as a His6-tagged fusion protein and purified by nickel-affinity chromatography. The protein was crystallized using the hanging-drop vapour-diffusion method in the presence of PEG 3000 as precipitant after treatment with hydrogen peroxide. X-ray diffraction data were collected to a maximum resolution of 2.4 A using a synchrotron-radiation source. The crystal belongs to the centred monoclinic space group C2, with unit-cell parameters a = 127.97, b = 135.41, c = 75.81 A, beta = 89.95 degrees. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress.

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Citations

May 20, 2006·Anais Da Academia Brasileira De Ciências·João A R G BarbosaRogério Meneghini
Oct 19, 2006·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Luis Eduardo Soares NettoBruno Brasil Horta
Aug 2, 2019·The Journal of Biological Chemistry·Daniela R TruzziOhara Augusto

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