4IP6

C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488A mutant

Summary for 4IP6

• Entry DOI: 10.2210/pdb4ip6/pdb
• Related: 4IP1
• Descriptor: Thiol:disulfide interchange protein DsbD (2 entities in total)
• Functional Keywords: thioredoxin, thiol:disulfide oxidoreductase, bacterial periplasm, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P36655
• Total number of polymer chains: 1
• Total formula weight: 14572.47

Authors

Saridakis, E.,Mavridou, D.A.I.,Redfield, C. (deposition date: 2013-01-09, release date: 2013-12-25, Last modification date: 2023-09-20)

Primary citation

Mavridou, D.A.,Saridakis, E.,Kritsiligkou, P.,Mozley, E.C.,Ferguson, S.J.,Redfield, C.
An Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold.
J.Biol.Chem., 289:8681-8696, 2014

PubMed Abstract: Proteins belonging to the thioredoxin (Trx) superfamily are abundant in all organisms. They share the same structural features, arranged in a seemingly simple fold, but they perform a multitude of functions in oxidative protein folding and electron transfer pathways. We use the C-terminal domain of the unique transmembrane reductant conductor DsbD as a model for an in-depth analysis of the factors controlling the reactivity of the Trx fold. We employ NMR spectroscopy, x-ray crystallography, mutagenesis, in vivo functional experiments applied to DsbD, and a comparative sequence analysis of Trx-fold proteins to determine the effect of residues in the vicinity of the active site on the ionization of the key nucleophilic cysteine of the -CXXC- motif. We show that the function and reactivity of Trx-fold proteins depend critically on the electrostatic features imposed by an extended active-site motif.

PubMed: 24469455
DOI: 10.1074/jbc.M113.513457

Experimental method

X-RAY DIFFRACTION (2.23 Å)