Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide
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-Å resolution tha...
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| Publicado en: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
National Academy of Sciences
2004
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC428440/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/15184683/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.0402769101 |
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