期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1978
卷号：75
期号：12
页码：5827-5830
DOI：10.1073/pnas.75.12.5827
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The three-dimensional structure of thioredoxin from bacteriophage T4 has been determined from a 2.8-angstrom resolution electron density map. Phase angles for this map were determined from one heavy atom derivative and anomalous differences from cadmium in the native crystals. The molecule of 87 amino acid residues is built up from two simple folding units; a betaalphabeta unit from the amino end of the chain and a betabetaalpha 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 have been correlated to differences in specificity towards the enzyme ribonucleotide reductase from different species.
