The Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA Enzymes

Oxidative protein folding in Gram-negative bacteria results in the formation of disulfide bonds between pairs of cysteine residues. This is a multistep process in which the dithiol-disulfide oxidoreductase enzyme, DsbA, plays a central role. The structure of DsbA comprises an all helical domain of u...

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Detalles Bibliográficos
Main Authors: Paxman, Jason J., Borg, Natalie A., Horne, James, Thompson, Philip E., Chin, Yanni, Sharma, Pooja, Simpson, Jamie S., Wielens, Jerome, Piek, Susannah, Kahler, Charlene M., Sakellaris, Harry, Pearce, Mary, Bottomley, Stephen P., Rossjohn, Jamie, Scanlon, Martin J.
Formato: Artigo
Idioma:Inglês
Publicado: American Society for Biochemistry and Molecular Biology 2009
Assuntos:
Protein Structure and Folding
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC2719422/
https://ncbi.nlm.nih.gov/pubmed/19389711
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.011502
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