Articles Related to homology
Different types of Glutaredoxins (GRXs) that play a major role in cellular anti-oxidative reactions have been studied for their structure and function from various organisms. Glutathione (GSH), an anti-oxidant with several medical benefits, binds to GRXs. This work has structurally characterized GRX2 from C. reinhardtii (CrGRX2) using biophysical, molecular modelling, and isothermal titration calorimetry (ITC) techniques. CrGRX2 adopts the classical GRX-Trx fold consisting of five β-strands surrounded by four α-helices that bind to GSH with moderate strength through a cysteine residue. The residues involved in the interaction closely match with those observed for E. coli and human counterparts, indicating that the cellular GSH-GRXs antioxidant system is highly conserved.
Mutation in a single nucleotide of a gene has the potential to change the structure and/or function of its protein. Albeit simply saying, it is not observed to be a general phenomenon. The effect of mutation is primarily determined by the stereochemical nature of the amino acid which has replaced the previous amino acid, resulting in the residue location being affected. Here we show that despite a change in the frequency of occurrence of a particular amino acid in a particular protein in different types of organisms, the overall function of the protein can still remain unaffected, even when the resultant protein conformation is relatively altered.