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The atypical thiol–disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase
Disulfide-bond-forming (DSB) oxidative folding enzymes are master regulators of virulence that are localized to the periplasm of many Gram-negative bacteria. The archetypal DSB machinery from Escherichia coli K-12 consists of a dithiol-oxidizing redox-relay pair (DsbA/B), a disulfide-isomerizing red...
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| Gepubliceerd in: | Acta Crystallogr D Struct Biol |
|---|---|
| Hoofdauteurs: | , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
International Union of Crystallography
2019
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6450060/ https://ncbi.nlm.nih.gov/pubmed/30950399 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2059798318018442 |
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