The Role of Dimerization on the Catalytic Properties of the Escherichia coli Disulfide Isomerase DsbC
نویسندگان
چکیده
Silvia A Arredondo, Tiffany F Chen, Austen F. Riggs, Hiram F Gilbert*, and George Georgiou 2, 3, 4 Departments of Chemical Engineering Biomedical Engineering, Molecular Genetics and Microbiology, Institute for Cell and Molecular Biology and Section of Neurobiology, School of Biological Sciences, University of Texas, Austin, TX 78712; and *Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030 Running Title: The Role of Dimerization in the Disulfide Isomerase DsbC Address correspondence to: George Georgiou, Ph.D. 1 University Station Stop C0400, Austin, TX 78712. Ph: 512-471-6975. Fax: 512-471-7963. E-mail: [email protected]
منابع مشابه
Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC.
The bacterial protein-disulfide isomerase DsbC is a homodimeric V-shaped enzyme that consists of a dimerization domain, two alpha-helical linkers, and two opposing thioredoxin fold catalytic domains. The functional significance of the two catalytic domains of DsbC is not well understood yet. We have engineered heterodimer-like DsbC derivatives covalently linked via (Gly(3)-Ser) flexible linkers...
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