Three-dimensional structure of thioredoxin induced by bacteriophage T4.

Publisher Website
Google Scholar
Abstract
The 3-dimensional structure of thioredoxin from bacteriophage T4 was determined from a 2.8 .ANG. resolution electron density map. Phase angles for this map were determined from 1 heavy atom derivative and anomalous differences from Cd in the native crystals. The molecule of 87 amino acid residues is built up from 2 simple folding units; a .beta..alpha..beta. unit from the amino end of the chain and a .beta..beta..alpha. unit from the carboxyl end. This structure is similar to that of thioredoxin from Escherichia coli in spite of their completely different amino acid sequences. The redox-active S-S bridge is part of a protrusion of the molecule as in E. coli thioredoxin, but with quite different surroundings. The structural differences in this region were correlated to differences in specificity towards the enzyme ribonucleotide reductase from different species [E. coli, yeast or calf liver].

This publication has 19 references indexed in Scilit: