1996. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell . EMBO J. 15 :2659–2667Chivers PT, Laboissiere MC, Raines RT. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J. 1996; 15 :2659–2667. [ PMC free ...
CXXC motif, a metal binding domain containing Cys-X-X-Cys motif, has been identified in various organisms. These proteins are capable of binding various types of heavy metals. In this study, heavy metal binding domain (CXXC motif) recombinant protein encoded from mcsA gene of S. aureus ...
The active-site CXXC motif of thiol:disulfide oxidoreductases is essential for their catalysis of redox reactions. Changing the XX residues can perturb the reduction potential of the active-site disulfide bond of the Escherichia coli enzymes thioredoxin (Trx; CGPC) and DsbA (CPHC). The reduction...
Two cysteines separated by two other residues (the CxxC motif) are employed by many redox proteins for formation, isomerization, and reduction of disulfide bonds and for other redox functions. The place of the C-terminal cysteine in this motif may be occupied by serine (the CxxS motif), mo...
Escherichia coli DsbB has four essential cysteine residues, among which Cys41 and Cys44 form a CXXC redox active site motif and the Cys104Cys130 disulfide bond oxidizes the active site cysteines of DsbA, the disulfide bond formation factor in the periplasm. Functional respiratory chain is requir...
APWCGPCK and APWCGHCK, however, did not display a even at a concentration 8 times higher than that of (APWCGHCK)8-MAP. It was assumed that a sterically proper proximity of at least two active site with CXXC motif was required for the expression of activity. 展开 ...
Mutating the conserved CXXC motif eliminated the protective effects against H2O2-induced apoptosis and diminished the protection of the mitochondria. However, the mutation of the other disulfide bond C91–C108 mainly preserved the protection of mitochondria by HSS, implying that the conserved CXXC ...
Our results demonstrate that this motif is important for protein folding, structural integrity, protein half-life and the stability of the Ero1-LâPDI complex. 展开 关键词: chaperones disulfide bonds endoplasmic reticulum protein folding redox ...
Mutating the conserved CXXC motif eliminated the protective effects against H2O2-induced apoptosis and diminished the protection of the mitochondria. However, the mutation of the other disulfide bond C91–C108 mainly preserved the protection of mitochondria by HSS, implying that the conserved CXXC ...
These stalks contain a highly evolutionarily conserved CXXC motif, whose function is unknown. To understand the function of these two conserved cysteines, we generated mice that lacked endogenous CD3ε but expressed a transgenic CD3ε molecule in which these cysteines were mutated to serines. Our...