Computational Analysis of 1XTC and Mutant 1XTC (D229E)



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This research is an investigation on the AB5 macromolecule secreted by Vibrio cholerae known as the cholera toxin (CT). We aim to document the effects of a mutation made on a key location on 1XTC crystal structure of cholera. Using several software, we created a D229E mutation in the 1XTC structure and recorded data on intermolecular interactions after equilibrating and simulating for 10 nanoseconds. The D229E mutation shows an increase in free energies along the A2 tail and instability in its structure by its decrease in hydrogen bonding and greater repulsive forces along the A2 tail. The same methods used in collecting data for 1XTC were used for two other forms of the AB5. One being the heat-labile enterotoxin, 1LTS which is a non-lethal AB5 toxin known to be secreted from E. coli, and the second being the elongated CT A2 tail structure, 1S5E.