3PFU

N-terminal domain of Thiol:disulfide interchange protein DsbD in its reduced form

Summary for 3PFU

• Entry DOI: 10.2210/pdb3pfu/pdb
• Related: 1JPE 1L6P 1VRS
• Descriptor: Thiol:disulfide interchange protein dsbD, 2,3-DIHYDROXY-1,4-DITHIOBUTANE (3 entities in total)
• Functional Keywords: immunoglobulin-like fold, thiol disulfide oxidoreductase, periplasmic domain of transmembrane protein, oxidoreductase, electron transport
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P36655
• Total number of polymer chains: 1
• Total formula weight: 15926.93

Authors

Mavridou, D.A.I.,Saridakis, E.,Ferguson, S.J.,Redfield, C. (deposition date: 2010-10-29, release date: 2011-05-04, Last modification date: 2023-11-01)

Primary citation

Mavridou, D.A.,Saridakis, E.,Kritsiligkou, P.,Goddard, A.D.,Stevens, J.M.,Ferguson, S.J.,Redfield, C.
Oxidation state-dependent protein-protein interactions in disulfide cascades
J.Biol.Chem., 286:24943-24956, 2011

PubMed 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.

PubMed: 21543317
DOI: 10.1074/jbc.M111.236141

Experimental method

X-RAY DIFFRACTION (1.8 Å)