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Submission Date
Winter 2021
Abstract
The bacteria E Coli infect approximately 200,000 individuals in the United States and can lead to critical illnesses. The transfer of iron from the bloodstream to bacteria is one of the main requirements for the survival. One of the mechanisms to obtain iron by use of siderophores and the protein FhuA was investigated. Undergraduate students grouped into teams to each explain a unique molecular story- modeled in Jmol/Pymol and demonstrated through a poster and PowerPoint. Using the PDB file, 2GRX, a drug to inhibit the TonB-Ton Box interaction which provides the FhuA iron mechanism energy to operate was researched. A protein model was designed to bind to the Ton Box region of FhuA with higher affinity by altering polar and charged residues to nonpolar or aliphatic residues that were present in the original TonB protein through programs Pymol and Jmol. The presence of many nonpolar amino acids in residues 8-16 and 588-592 of FhuA and the charged amino acids in residues 166-170 and 225-235 of TonB suggest that mutations of R166F, N227L, K231A on the tonB will lead to a protein with a stronger interaction with the Ton Box. The change from Arginine 166 to Phenlyalanine facilitates a nonpolar-nonpolar interaction between the TonB and Alanine of FhuA. Similarly, mutating polar asparagine to nonpolar leucine and the change of positively charged Lysine to uncharged Alanine will allow a stronger interaction. These hypothesized interactions of the mutated Anti-TonB1 with the FhuA are based on predicted outcomes because of the limitations of programmed docking of large proteins. Through the research and design of the course, students were able to develop skills with protein interface programs such as Pymol, Jmol, and Pyrx. This project was made possible by Nova Southeastern University and the guidance from Dr. Arthur Sikora and Dr. Emily Schmitt Lavin.
Recommended Citation
Diaz, Jose; Luib, Ryan; and Doki, Seethal, "Limiting Iron Acquisition of E. Coli With Anti-TonB1 and AntiTonB2" (2021). Protein Modeling Reports. 2.
https://nsuworks.nova.edu/protein_modeling_reports/2