Mavridou, D.A.I and Saridakis, E and Kritsiligkou, P and Goddard, Alan and Stevens, J.M and Ferguson, S.J and Redfield, C (2011) Oxidation state-dependent protein-protein interactions in disulfide cascades. Journal of Biological Chemistry, 286 (28). pp. 24943-24956. ISSN 0021-9258Full text not available from this repository.
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.
|Subjects:||C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry|
|Divisions:||College of Sciences > Faculty of Science > School of Life Sciences|
|Depositing User:||Alan Goddard|
|Date Deposited:||16 Nov 2012 11:51|
|Last Modified:||08 May 2013 15:23|
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