Conformational and functional similarities between glutaredoxin and thioredoxins.
AUTOR(ES)
Eklund, H
RESUMO
The tertiary structures of thioredoxin from Escherichia coli and bacteriophage T4 have been compared and aligned giving a common fold of 68 C alpha atoms with a root mean square difference of 2.6 A. The amino acid sequence of glutaredoxin has been aligned to those of the thioredoxins assuming that glutaredoxin has the same common fold. A model of the glutaredoxin molecule was built on a vector display using this alignment and the T4 thioredoxin tertiary structure. By comparison of the model with those of the thioredoxins, we have identified a molecular surface area on one side of the redox-active S-S bridge which we suggest is the binding area of these molecules for redox interactions with other proteins. This area comprises residues 33-34, 75-76 and 91-93 in E. coli thioredoxin; 15-16, 65-66 and 76-78 in T4 thioredoxin and 12-13, 59-60 and 69-71 in glutaredoxin. In all three molecules, this part of the surface is flat and hydrophobic. Charged groups are completely absent. In contrast, there is a cluster of charged groups on the other side of the S-S bridge which we suggest participates in the mechanisms of the redox reactions. In particular, a lysine residue close to an aromatic ring is conserved in all molecules.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=557542Documentos Relacionados
- Identification of functional similarities between proteins using directed evolution
- In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
- Structural and functional similarities between the promoters for mouse tenascin and chicken cytotactin.
- The conformational basis of energy conservation in membrane systems. II. Correlation between conformational change and functional states.
- Functional Similarities between the icm/dot Pathogenesis Systems of Coxiella burnetii and Legionella pneumophila