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

  Publikacja

  • 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 - Rok 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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