Escherichia coli thioredoxin

Dillet V, Dyson HJ, Bashford D (1998) Calculations of electrostatic interactions and pKas in the active site of Escherichia coli thioredoxin. Biochemistry 37 10298-10306. 

Langsetmo K, Fuchs JA, Woodward C (1991) The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. its titration produces a related shift in global stability Biochemistry 30 7603-7609. 

Escherichia coli thioredoxin reductase refined at 2 A resolution. Implication of a large conformational change during catalysis. Journal of Molecular Biology, 236, 800-16. 

Tabor, S., Huber, H. E., and Richardson, C. C. (1987). Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7./. Biol. Chem. 262, 16212-16223. 

M. F. Jeng, A. P. Campbell, T. Begley, A. Holmgren, D. A. Case, P. E. Wright and H. J. Dyson, High resolution solution structures of oxidized and reduced escherichia-coli thioredoxin. Structure, 2(9), 853-868 (1994). 

Wilson, N., E. Barbar, J. Fuchs, and C. Woodward. Aspartic Acid in Reduced Escherichia coli Thioredoxin Has a p 9. Biochem. 34, 8931-8939 (1995). [A research report on a remarkably high value for a specific amino acid in a protein.]... 

LeMaster, D.M. Structural determinants of the catalytic reactivity of the buried cysteine of Escherichia coli thioredoxin. Biochemistry 1996, 35,14876-81. 

The endoplasmic reticulum PDl, which catalyzes the reduction, oxidation, and reshufSing of protein disulfides in eukaryotes, is a homodimer of two 57 kDa subunits. Each subunit contains two functional domains with significant sequence homology to Escherichia coli thioredoxin. The functional equivalent of PDI in prokaryotes, DsbA, is a periplasmic, monomeric protein characterized by a low similarity to E. coli thioredoxin with the active site sequence motif CPHC. ... 

Kim, M.Y., Maier, C.S., Reed, D.J., et al. (2001) Intramolecular interactions in chemically modified Escherichia coli thioredoxin monitored by hydrogen/deuterium exchange and electrospray ionization mass spectrometry. Biochemistry, 40 (48), 14413-14421. 

We present the first primary structiire of a f-type thioredoxin from plants. This protein which has a blocked N-terminus shows only 24% residue identities with spinach thioredoxin m or Escherichia coli thioredoxin. A third Cys present may have some function in the interaction between thioredoxin f and target enzyme. 

The equilibrium unfolding of the oxidized form of Escherichia coli thioredoxin at pH 7 was studied by Santoro and Bolen [1] using guanidine hydrochloride (GdnHCl) and urea as denaturant at 25°C by monitoring the changes in ellipticity at 222nm. 

Soderberg B O, Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A... 

Svergun et al. [138] studied three proteins lysozyme, Escherichia coli thioredoxin reductase, and E. coli ribonucleotide reductase protein Rl, in aqueous solution, using x-ray and neutron scattering. The density of the water of the first hydiadon shell of these proteins differed from that of bulk water, the average relative deusities were 1.08 0.02, 1.16 0.05, and 1.12 0.06. These experimental values are smaller than those calculated from the packing, 1.22 according to Gerstein and Chothia [137], but still appreciable. 

H. J. Dyson, L. L. Tennant, and A. Holmgren, Biochemistry, 30, 4262 (1991). Proton-Transfer Effects in the Active-Site Region of Escherichia coli Thioredoxin Using Two-Dimensional H NMR. 

Chinn, P. C. Pigiet, V Fahey, R. C. Determination of thiol proteins using monobromobimane labebng and high-performance liquid chromatographic analysis application to Escherichia coli thioredoxin. Anal. Biochem. 1986, 159, 143-149. 

Escherichia coli thioredoxin has characteristic sites which are affected by the transformation between its... 

Mammalian thioredoxin reductase is able to reduce many substances in addition to thioredoxin such as insulin, vitamin K, alloxan, and others, while Escherichia coli enzyme is a... 

Bartolucci, S., A. Guagliardi, E. Pedone, D. De Pascale, R. Cannio, L. Camardella, M. Rossi, G. Nicastro, C. de Chiara, P. Facci, G. Mascetti, and C. Nicolini. 1997. Thioredoxin from Bacillus acidocaldarius characterization, high-level expression in Escherichia coli and molecular modelling. Biochem J 328 277-285. 

Yasukawa T, Kanei-Ishii C, Maekawa T, Eujimoto J, Yamamoto T, Ishii S. (1995) Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. J Biol Chem 270, 25328-31. 

Lu, Z., Murray, K. S., Van Cleave, V., LaVallie, E. R., Stahl, M. L., and McCoy, J. M. (1995) Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin a system designed for exploring protein-protein interactions. Biotechnology 13, 366-372. 

Mao, S. S., Yu, G. X., Chalfoun, D., and Stubbe, J., 1992, Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity, Biochemistry 31 9752n9759. 

Jordan, A., slund, F., Pontis, E., Reichard, P., and Holmgren, A., 1997, Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile. J. Biol. Chem. 272 18044918050. 

High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with 80. 

Thioredoxin from Escherichia coli is a small ubiquitous protein with of 11,700 which contains a redox-active cystine moiety on an exposed jS-reverse-turn . It can... 

Thioredoxin from E. coli has been studied extensively using biochemical, spectroscopic and X-ray diffraction techniques. The protein consists of a single polypeptide chain of 108 amino acid residues of known sequence. The protein has been cloned and expressed. Thioredoxin of E. coli is a compact molecule with 90% of its residues in hehces, beta-strands or reverse turns. This protein transports electrons via an oxidation-reduction active disulfide". The oxidized form thioredoxin-(S2) is reduced to thioredoxin-(SH)2. In particular, this protein was found to participate in the reduction of ribonucleotides to deoxyribonucleotides. In Fig. 1, the optimized stracture is shown with a carbon backbone for clarity only. The molecule consists of two conformational domains, connected by two helices. The beta-sheet forms the core of the molecule packed on either side by clusters of hydrophobic residues. Helices form the external surface. We used a crystal stracture of the oxidized form of thioredoxin from Escherichia coli that has been refined by the stereochemically restrained least-squares procedure at 1.68 A resolution". ... 

Katti, S. K., LeMaster, D. M., Eklund, H., Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution, JATo/. Biol. 212, 167 (1990). 

Regeneration of the ribonucleotide reductase is accomplished in Escherichia coli and in mammals by thioredoxin, a dithiol polypeptide (M.W. 12,000) coenzyme, which also plays a role in other protein disulfide reductase reactions. In thioredoxin, two cysteine residues in the sequence -Cys-Gly-Pro-Cys are converted to cystine. Reduced thioredoxin is regenerated by thioredoxin reductase, a flavoprotein enzyme that uses NADPH + H+. 

Prinz, W. A., Aslund, F., Holmgren, A., and Beckwith, J. (1997). The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm./. Biol. Chem. 272, 15661-15667. 

A set of hybrid proteins containing the Ap40 peptide domain and dimeric glucose dehydrogenase (GDH) or thioredoxin (Trx) have been constructed in present work. Expression and purification of the proteins was accomplished using prokaryotic system based on Escherichia coli. Details of the construction and expression of hybrid proteins are subject of special report and will be presented elsewhere. Hen egg lysozyme was fibrilized as described in our recent work. 

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