Year: 2011
Type: article
Abstract: Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms.
Source: Journal of Biological Chemistry
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Awards: Defining protein-protein interaction networks in cytochrome c assembly., Probing the activities of the Ccm proteins of the cytochrome c biosynthesis system, Bacterial transport and transformation of nitrate and nitrite in the nitrogen cycle, Nuclear magnetic resonance spectroscopy as a tool to study the structure, function, dynamics and folding of proteins: University Award for a research technologist in biomolecular NMR.
OpenAlex ID: W2082663705