Pyridoxal Phosphatase Conclusion

In conclusion, the results suggested that the team is on the right track, in terms of characterizing the protein. In the evolutionary component of this paper, the conserved regions obtained from Multiple Sequence Alignment (MSA) was visualized using PyMOL. This gave the team a rough idea on the location of 2cfsA's catalytic site. Evolutionary relatedness was then characterised through the creation of a phylogenetic tree. During the structural component, based on the information obtained from Almo et al., 2007, and PDBsum (the LIGPLOTs, in particular), PyMOL was once again used to generate a three dimensional view of the protein's catalytic site. Similarities between both visualizations supported the theory that the suggested catalytic site could indeed be the actual one. Functional prediction using structure reaffirms 2cfsA's function as a hydrolase while prediction base on protein-protein interactions revealed that 2cfsA possibly plays a role in protein folding as well as being a coenzyme for asparagine synthetase. Further studies focussing on regulation and expression levels of 2cfsA will likely shed new light on more roles of 2cfsA in human cellular homeostasis.