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

Discola, Karen Fulan ; Alves, Simone Vidigal ; De Oliveira, Marcos Antonio ; Barbosa, João Alexandre Ribeiro Gonçalves ; Medrano, Francisco Javier ; Netto, Luis Eduardo Soares ; Guimarães, Beatriz Gomes

Acta crystallographica. Section F, Structural biology and crystallization communications, 2005-04, Vol.61 (4), p.387-390 [Periódico revisado por pares]

5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers

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Título:
Crystallization and preliminary X-ray diffraction analysis of NADPH-dependent thioredoxin reductase I from Saccharomyces cerevisiae
Autor: Discola, Karen Fulan ; Alves, Simone Vidigal ; De Oliveira, Marcos Antonio ; Barbosa, João Alexandre Ribeiro Gonçalves ; Medrano, Francisco Javier ; Netto, Luis Eduardo Soares ; Guimarães, Beatriz Gomes
Assuntos: AFFINITY ; Cloning, Molecular ; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY ; CRYSTAL STRUCTURE ; CRYSTALLIZATION ; Crystallization - methods ; Crystallization Communications ; CRYSTALS ; DIFFUSION ; ESCHERICHIA COLI ; Histidine ; HYDROGEN PEROXIDE ; NICKEL ; Polyethylene Glycols ; Polymerase Chain Reaction ; PYRIDINE ; Recombinant Fusion Proteins ; REDUCTION ; RESOLUTION ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins - chemistry ; SPACE GROUPS ; thioredoxin reductase I (TRR1) ; Thioredoxin-Disulfide Reductase - chemistry ; Volatilization ; X-RAY DIFFRACTION
É parte de: Acta crystallographica. Section F, Structural biology and crystallization communications, 2005-04, Vol.61 (4), p.387-390
Notas: ark:/67375/WNG-RNS111ZC-K
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ArticleID:AYF2LL5016
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: 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 Å 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 Å, β = 89.95°. The crystal structure was solved by molecular‐replacement methods and structure refinement is in progress.
Editor: 5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers
Idioma: Inglês

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

Discola, Karen Fulan ; Alves, Simone Vidigal ; De Oliveira, Marcos Antonio ; Barbosa, João Alexandre Ribeiro Gonçalves ; Medrano, Francisco Javier ; Netto, Luis Eduardo Soares ; Guimarães, Beatriz Gomes

5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers

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