Clever design of a water-soluble variant of the integral membrane protein DsbB that is able to catalyze disulfide bond formation in the Escherichia coli cytoplasm
In Dario Mizrachi's recent Nature Chemical Biology paper, we describe the design of a water-soluble variant of the integral membrane protein DsbB. The co-expression of this DsbB variant with an export-defective copy of DsbA facilitates disulfide-bond formation in the Escherichia coli cytoplasm in a quinone-dependent fashion. The paper was the feature of a News and Views article in Nature Chemical Biology authored entitled "Protein Engineering: Redirecting Protein Machinery" by Kalistyn Burley and Celia Goulding.
You can download our paper here:
or read more about the work in the related Cornell Chronicle article: