Ontology highlight
ABSTRACT:
SUBMITTER: Heras B
PROVIDER: S-EPMC428440 | biostudies-literature | 2004 Jun
REPOSITORIES: biostudies-literature
Heras Begoña B Edeling Melissa A MA Schirra Horst J HJ Raina Satish S Martin Jennifer L JL
Proceedings of the National Academy of Sciences of the United States of America 20040607 24
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 1.7and 2.0-A resolution that are meant to represent the reduced and oxidized forms, respectively. The oxidized structure, however, reveals a mixture of both redox forms, suggesting that oxidized DsbG is less stable than the red ...[more]