Structural highlights
Function
DSBD_ECOLI Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399]
Publication Abstract from PubMed
Proteins belonging to the thioredoxin 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 (cDsbD) 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.
An Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold.,Mavridou DA, Saridakis E, Kritsiligkou P, Mozley EC, Ferguson SJ, Redfield C J Biol Chem. 2014 Jan 27. PMID:24469455[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mavridou DA, Saridakis E, Kritsiligkou P, Mozley EC, Ferguson SJ, Redfield C. An Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold. J Biol Chem. 2014 Jan 27. PMID:24469455 doi:http://dx.doi.org/10.1074/jbc.M113.513457
