ATP binding domain 4 Conclusion
It was found that ATP Binding Domain 4 sequence is conserved across species in Domain Archaea and Eukarya suggesting that this protein has very important functions. Being a type of N-type ATP pyrophosphatase, is important for energy metabolism, since pyrophosphatases catalyse the cleavage of ATP alpha-beta phosphodiester bond to form AMP and pyrophosphate. The ratio between ATP and AMP is used as a way for a cell to sense how much energy is available and control the metabolic pathways that produce and consume ATP. Therefore, knowing how ATP binding domain 4 is extremely important in studying energy metabolism and signalling of cells. Improvement in this research in terms of further structural comparison of well-known pyrophosphatases and determination of actual ligand based on experimental data may help in the finding of our protein’s functions. Due to time constrains in this study, experiment comparison between PP loops of other ATP pyrophosphatases was not possible, such as PAPS synthetases. This study has highlighted potential important residues of ATP binding domain 4 in Pyrococcus furiosus like Gly(13), Gly(14), Ser(17), Ala(20), Gln(46). Those corresponding equivalent residues in human ATP binding domain 4 should be identified and investigate for it therapeutical value on medical research.