The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed-disulfide intermediate between thioredoxin and the substrate. In order to model the interaction, we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue. A specific covalent complex has been prepared between the remaining cysteine residue and a short cysteine-containing peptide. This paper describes the preparation and characterization of the mutant protein both free and in the peptide complex.
[NMR paper] NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in so
NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
Related Articles NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
Protein Sci. 2005 Apr;14(4):1082-90
Authors: Wang G, Peterkofsky A, Keifer PA, Li X
The solution form of IIA(Ntr) from Escherichia coli and its interaction with its partner protein, NPr, were characterized by nuclear magnetic resonance (NMR)...
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[NMR paper] NMR analysis of cleaved Escherichia coli thioredoxin (1-73/74-108) and its P76A varia
NMR analysis of cleaved Escherichia coli thioredoxin (1-73/74-108) and its P76A variant: cis/trans peptide isomerization.
Related Articles NMR analysis of cleaved Escherichia coli thioredoxin (1-73/74-108) and its P76A variant: cis/trans peptide isomerization.
Protein Sci. 2000 Jan;9(1):20-8
Authors: Yu WF, Tung CS, Wang H, Tasayco ML
Inspection of high resolution three-dimensional (3D) structures from the protein database reveals an increasing number of cis-Xaa-Pro and cis-Xaa-Yaa peptide bonds. However, we are still far from being able to...
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[NMR paper] Oligomerization of the EK18 mutant of the trp repressor of Escherichia coli as observ
Oligomerization of the EK18 mutant of the trp repressor of Escherichia coli as observed by NMR spectroscopy.
Related Articles Oligomerization of the EK18 mutant of the trp repressor of Escherichia coli as observed by NMR spectroscopy.
Arch Biochem Biophys. 1999 Nov 1;371(1):35-40
Authors: Chae YK, Abildgaard F, Royer CA, Markley JL
The regulation of the trp repressor system of Escherichia coli is frequently modeled by a single equilibrium, that between the aporepressor (TR) and the corepressor, l-tryptophan (Trp), at their intracellular...
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[NMR paper] Glucose transporter of Escherichia coli: NMR characterization of the phosphocysteine
Glucose transporter of Escherichia coli: NMR characterization of the phosphocysteine form of the IIB(Glc) domain and its binding interface with the IIA(Glc) subunit.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Glucose transporter of Escherichia coli: NMR characterization of the phosphocysteine form of the IIB(Glc) domain and its binding interface with the IIA(Glc) subunit.
Biochemistry. 1997 Jun 17;36(24):7408-17
Authors: Gemmecker G, Eberstadt M, Buhr A, Lanz R, Grdadolnik SG, Kessler H, Erni B...
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[NMR paper] Glucose transporter of Escherichia coli: NMR characterization of the phosphocysteine
Glucose transporter of Escherichia coli: NMR characterization of the phosphocysteine form of the IIB(Glc) domain and its binding interface with the IIA(Glc) subunit.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Glucose transporter of Escherichia coli: NMR characterization of the phosphocysteine form of the IIB(Glc) domain and its binding interface with the IIA(Glc) subunit.
Biochemistry. 1997 Jun 17;36(24):7408-17
Authors: Gemmecker G, Eberstadt M, Buhr A, Lanz R, Grdadolnik SG, Kessler H, Erni B...
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[NMR paper] Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredox
Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein.
Related Articles Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein.
FEBS Lett. 1994 Feb 14;339(1-2):11-7
Authors: Dyson HJ, Jeng MF, Model P, Holmgren A
A mutant of Escherichia coli thioredoxin containing serine residues in place of the two active-site cysteines, termed C32S,C35S, previously shown to be...
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[NMR paper] Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredox
Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein.
Related Articles Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein.
FEBS Lett. 1994 Feb 14;339(1-2):11-7
Authors: Dyson HJ, Jeng MF, Model P, Holmgren A
A mutant of Escherichia coli thioredoxin containing serine residues in place of the two active-site cysteines, termed C32S,C35S, previously shown to be...
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08-22-2010 03:33 AM
[NMR paper] Proton-transfer effects in the active-site region of Escherichia coli thioredoxin usi
Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
Related Articles Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
Biochemistry. 1991 Apr 30;30(17):4262-8
Authors: Dyson HJ, Tennant LL, Holmgren A
A series of two-dimensional (2D) correlated 1H NMR spectra of reduced and oxidized Escherichia coli thioredoxin have been used to probe the effects of pH in the vicinity of the active site, -Cys32-Gly-Pro-Cys35-, using the...