4IP1
C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488K mutant
Summary for 4IP1
| Entry DOI | 10.2210/pdb4ip1/pdb |
| Related | 4IP6 |
| 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 | 14630.58 |
| Authors | Saridakis, E.,Mavridou, D.A.I.,Redfield, C. (deposition date: 2013-01-09, release date: 2013-12-25, Last modification date: 2024-11-20) |
| 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 Cited by 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: 24469455DOI: 10.1074/jbc.M113.513457 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.47 Å) |
Structure validation
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