3pfu

Publication Abstract from PubMed

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.

Oxidation state-dependent protein-protein interactions in disulfide cascades.,Mavridou DA, Saridakis E, Kritsiligkou P, Goddard AD, Stevens JM, Ferguson SJ, Redfield C J Biol Chem. 2011 Jul 15;286(28):24943-56. Epub 2011 May 3. PMID:21543317^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.