טוען...
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...
שמור ב:
| הוצא לאור ב: | J Biol Chem |
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| Main Authors: | , , , , , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
American Society for Biochemistry and Molecular Biology
2018
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| נושאים: | |
| גישה מקוונת: | 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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