Search results for: DISULFIDE ISOMERASE

• Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide

  Publication

  • B. Heras
  • M. A. Edeling
  • H. J. Schirra
  • S. Raina
  • J. L. Martin

  - PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA - Year 2004

  Dsb proteins control the formation and rearrangement of disulfide bonds during the folding of secreted and membrane proteins in bacteria. DsbG, a member of this family, has disulfide bond isomerase and chaperone activity. Here, we present two crystal structures of DsbG at 1.7- and 2.0-Angstrom resolution that are meant to represent the reduced and oxidized forms, respectively. The oxidized structure, however, reveals a mixture...

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• Impact of selected amino acids of HP0377 (Helicobacter pylori thiol oxidoreductase) on its functioning as a CcmG (cytochrome c maturation) protein and Dsb (disulfide bond) isomerase

  Publication

  • M. Grzeszczuk
  • A. Bąk
  • A. Banaś
  • P. Urbanowicz
  • S. Dunin-Horkawicz
  • A. Gieldon
  • C. Czaplewski
  • A. Liwo
  • E. Jagusztyn-Krynicka

  - PLOS ONE - Year 2018

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• Dehydration converts DsbG crystal diffraction from low to high resolution

  Publication

  • B. Heras
  • M. A. Edeling
  • K. A. Byriel
  • A. Jones
  • S. Raina
  • J. L. Martin

  - STRUCTURE - Year 2003

  Diffraction quality crystals are essential for crystallographic studies of protein structure, and the production of poorly diffracting crystals is often regarded as a dead end in the process. Here we show a dramatic improvement of poorly diffracting DsbG crystals allowing high-resolution diffraction data measurement. Before dehydration, the crystals are fragile and the diffraction pattern is streaky, extending to 10 Å resolution....

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