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Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB

Correct disulfide bond formation is essential for proper folding of many proteins, including bacterial virulence factors. The suppressor of copper sensitivity (Scs) proteins have roles in dithiol/disulfide interchange and the bacterial response to copper stress. Encoded in a four-gene cassette (ScsA...

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Shranjeno v:
Bibliografske podrobnosti
izdano v:J Biol Chem
Main Authors: Furlong, Emily J., Choudhury, Hassanul G., Kurth, Fabian, Duff, Anthony P., Whitten, Andrew E., Martin, Jennifer L.
Format: Artigo
Jezik:Inglês
Izdano: American Society for Biochemistry and Molecular Biology 2018
Teme:
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC5912455/
https://ncbi.nlm.nih.gov/pubmed/29491145
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.001860
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