Related ArticlesProton-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 complete proton resonance assignments available for thioredoxin. In either oxidation state, the majority of residues of the thioredoxin molecule remain unchanged between pH 5.7 and pH 10, as indicated by the identical chemical shifts of the C alpha H, C beta H, and other protons. In reduced thioredoxin, a fairly widespread region around the active-site dithiol is affected by the titration of a group or groups with pKa approximately 7.1-7.4 in 2H2O. Another titration, with pKa approximately 8.4, affects a smaller region of the protein. Oxidized thioredoxin contains a disulfide and no free thiol groups; nevertheless, the proton resonances of many groups in the active-site region were observed to titrate with a pKa of 7.5, probably as a result of an abnormally high pKa value for the carboxyl group of the buried Asp-26 residue. For reduced thioredoxin, the results indicate that Asp-26 is titrating in this pH range, as well as both thiol groups. The new results are strongly suggestive that the mechanism of thioredoxin-catalyzed protein disulfide reduction may be critically dependent on proton transfer as well as electron transfer within the active site.
[NMR paper] Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase reveal
Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy.
Related Articles Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy.
J Am Chem Soc. 2005 Jun 15;127(23):8424-32
Authors: Wu J, Bell AF, Jaye AA, Tonge PJ
Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes the flavin-dependent oxidation of fatty acyl-CoAs to the corresponding trans-2-enoyl-CoAs. The interaction of hexadienoyl-CoA (HD-CoA), a product analogue, with recombinant pig...
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[NMR paper] High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli d
High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase.
Related Articles High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase.
Biochemistry. 2000 Oct 24;39(42):12789-95
Authors: Kitahara R, Sareth S, Yamada H, Ohmae E, Gekko K, Akasaka K
A high-pressure (15)N/(1)H two-dimensional NMR study has been carried out on folate-bound dihydrofolate reductase (DHFR) from Escherichia coli in the pressure range between 30 and 2000 bar. Several...
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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] Proton NMR investigation of the heme active site structure of an engineered cytochrom
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Related Articles Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Biochemistry. 1999 Jul 13;38(28):9146-57
Authors: Wang X, Lu Y
The heme active site structure of an engineered cytochrome c peroxidase that closely mimics manganese peroxidase (MnP) has been characterized by both one- and two-dimensional NMR spectroscopy. All...
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[NMR paper] NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and
NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Related Articles NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Eur J Biochem. 1998 Oct 15;257(2):299-308
Authors: Jeng MF, Reymond MT, Tennant LL, Holmgren A, Dyson HJ
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...
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[NMR paper] NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli Dna
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
J Mol Biol. 1996 Jul 12;260(2):236-50
Authors: Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K
The recombinant N-terminal 107-amino acid polypeptide fragment 2-108 of the DnaJ molecular chaperone of Escherichia...
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[NMR paper] The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli pho
The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.
FEBS Lett. 1993 Jan 2;315(1):11-5
Authors: van Nuland NA, Kroon GJ, Dijkstra K, Wolters GK, Scheek RM, Robillard GT
The region of the surface of...
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[NMR paper] Motional effects on NMR structural data. Comparison of spinach and Escherichia coli a
Motional effects on NMR structural data. Comparison of spinach and Escherichia coli acyl carrier proteins.
Related Articles Motional effects on NMR structural data. Comparison of spinach and Escherichia coli acyl carrier proteins.
Biochem Pharmacol. 1990 Jul 1;40(1):7-13
Authors: Kim Y, Ohlrogge JB, Prestegard JH
Proteins in solution need not exist in a single rigid structure but can exist in a dynamic equilibrium among structural forms. The problems that this poses for structure determination using nuclear Overhauser effect data from...