Escherichia coli thioredoxin from

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. 

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. 

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. 

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). 

Katti S K, LeMaster D M, Crystal structure of thioredoxin from Escherichia coli at 1.68A... 

Holmgren, A. Reversible Chemical Modification of the Tryptophan Residues of Thioredoxin from Escherichia coli B. Eur. J. Biochem. 26, 528-534 (1972). 

Effects of Oxidation of Tryptophan Residues in Thioredoxin from Escherichia coli by N-Bromosuccinimide. J. Biol. Chem. 248, 4106-4111 (1973). 

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