Molecular Visualization Laboratory (BIOL4450): Molecular Visualization of Phosphoethanolamine Methyltransferase from Plasmodium falciparum
Disciplines
Biochemistry, Biophysics, and Structural Biology | Laboratory and Basic Science Research | Molecular Biology | Plant Biology | Research Methods in Life Sciences | Science and Mathematics Education
Abstract (300 words maximum)
Malaria is a major worldwide health threat as this disease, caused by different species of Plasmodium parasites, results in over 1 million deaths and 300 million clinical cases each year. Due to the large negative impacts which Malaria has on humanity, it is important to research and identify novel biochemical pathways that avoid drug resistance. One such pathway that has potential to highlight specific drug targets is the phosphobase methylation pathway which synthesizes phosphocholine, a precursor of phosphatidylcholine. A key enzyme of this pathway, specific to Plasmodium falciparum, is the phosphoethanolamine methyltransferase (PfPMT) enzyme which is responsible for sequential methylation reactions. PfPMT holds a unique 3D structure when compared to its other forms found in plants and protists making it a novel target for drug development. Specifically, the conformation of PfPMT in complexed with phosphoethanolamine (pEA) and S-adenosylhomocysteine (SAH) provides insights into the structure and function of its active site. In the Molecular Visualization Laboratory (BIOL4450) class at KSU, to gain a better understanding of the PfPMT 3D structure, biochemical methods such as site-directed mutagenesis and protein purification were used to perform X-ray crystallography. Additionally, X-ray crystallography experiments were conducted as a vital source to collect information on the 3D structures of PMT and interactions with ligands. Finally, the 3D structure of PfPMT was visualized and analyzed using a series of tools, including virtual reality (VR), augmented reality (AR), and 3D printing, to contribute to the field of STEAM (science, technology, engineering, art, and math) and improve academic understanding of protein biochemistry. Through use of biochemical techniques and direct analysis of 3D visualization methods of PMT will contribute to a greater understanding of its active site function and structure. With new insights on PMT 3D structure and function, novel drug approaches may be developed in the future.
Academic department under which the project should be listed
CSM - Molecular and Cellular Biology
Primary Investigator (PI) Name
Dr. Soon Goo Lee
Molecular Visualization Laboratory (BIOL4450): Molecular Visualization of Phosphoethanolamine Methyltransferase from Plasmodium falciparum
Malaria is a major worldwide health threat as this disease, caused by different species of Plasmodium parasites, results in over 1 million deaths and 300 million clinical cases each year. Due to the large negative impacts which Malaria has on humanity, it is important to research and identify novel biochemical pathways that avoid drug resistance. One such pathway that has potential to highlight specific drug targets is the phosphobase methylation pathway which synthesizes phosphocholine, a precursor of phosphatidylcholine. A key enzyme of this pathway, specific to Plasmodium falciparum, is the phosphoethanolamine methyltransferase (PfPMT) enzyme which is responsible for sequential methylation reactions. PfPMT holds a unique 3D structure when compared to its other forms found in plants and protists making it a novel target for drug development. Specifically, the conformation of PfPMT in complexed with phosphoethanolamine (pEA) and S-adenosylhomocysteine (SAH) provides insights into the structure and function of its active site. In the Molecular Visualization Laboratory (BIOL4450) class at KSU, to gain a better understanding of the PfPMT 3D structure, biochemical methods such as site-directed mutagenesis and protein purification were used to perform X-ray crystallography. Additionally, X-ray crystallography experiments were conducted as a vital source to collect information on the 3D structures of PMT and interactions with ligands. Finally, the 3D structure of PfPMT was visualized and analyzed using a series of tools, including virtual reality (VR), augmented reality (AR), and 3D printing, to contribute to the field of STEAM (science, technology, engineering, art, and math) and improve academic understanding of protein biochemistry. Through use of biochemical techniques and direct analysis of 3D visualization methods of PMT will contribute to a greater understanding of its active site function and structure. With new insights on PMT 3D structure and function, novel drug approaches may be developed in the future.