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Results: 3

1.
FIGURE 1.

FIGURE 1. From: De Novo Design and Evolution of Artificial Disulfide Isomerase Enzymes Analogous to the Bacterial DsbC.

A, structures of DsbC, DsbG, and PDI exhibit similar domain arrangement. B, protein structures of DsbA and FkpA, and a predictive molecular model of FkpA-DsbA2. The amino acid sequence at the fusion region of the two proteins is shown.

Silvia Arredondo, et al. J Biol Chem. 2008 November 14;283(46):31469-31476.
2.
FIGURE 3.

FIGURE 3. From: De Novo Design and Evolution of Artificial Disulfide Isomerase Enzymes Analogous to the Bacterial DsbC.

FkpA-DsbA2 mutants obtained following mutagenesis and selection for CuCl2 resistance. A, molecular model of the FkpA-DsbA2m18 mutant. B, yield of active vtPA in E. coli PB351 (SF100 ΔdsbC) obtained as described in Fig. 2A. C, AppA activity assayed as described under “Experimental Procedures.” The AppA activity was determined by measuring A410. One unit was defined as 1,000 × A410 per min/ml (4).

Silvia Arredondo, et al. J Biol Chem. 2008 November 14;283(46):31469-31476.
3.
FIGURE 2.

FIGURE 2. From: De Novo Design and Evolution of Artificial Disulfide Isomerase Enzymes Analogous to the Bacterial DsbC.

Disulfide-bond formation in vivo. A, yield of active vtPA in dsbC (gray bars) or dsbA (black bars) cells. E. coli PB351 and PB401 (respectively) were transformed with pTrcStIIvtPA and pBAD derivatives encoding the respective FkpA-DsbA fusion proteins and grown in LB media. Protein synthesis was induced as described under “Experimental Procedures,” and the yield of active vtPA was determined 3 h after induction. Relative activities were obtained by dividing the ΔA405 of each strain (subtracted of the background consisting of a strain not expressing vtPA) by the ΔA405 of a strain expressing vtPA alone. B, PhoA activity in E. coli MC1000 dsbA (white bars) and MC1000 dsbB (black bars). The alkaline phosphatase activity in the parental isogenic strain MC1000 is shown by the gray bar.

Silvia Arredondo, et al. J Biol Chem. 2008 November 14;283(46):31469-31476.

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