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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Detalles Bibliográficos
Autores principales: Walden, Patricia M., Whitten, Andrew E., Premkumar, Lakshmanane, Halili, Maria A., Heras, Begoña, King, Gordon J., Martin, Jennifer L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2019
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6450060/
https://www.ncbi.nlm.nih.gov/pubmed/30950399
http://dx.doi.org/10.1107/S2059798318018442

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6450060/
https://www.ncbi.nlm.nih.gov/pubmed/30950399
http://dx.doi.org/10.1107/S2059798318018442

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