Class
Article
College
College of Science
Department
Chemistry and Biochemistry Department
Faculty Mentor
Sean Johnson
Presentation Type
Poster Presentation
Abstract
Protein tyrosine phosphatases (PTPs) regulate cell signaling by removing phosphate groups from tyrosine residues. Malfunction of these enzymes can lead to diseases such as diabetes and cancer. A conserved feature among PTPs is the catalytic acid loop, essential for phosphate removal. Computational analysis of PTP structures revealed that ancestral PTPs have considerable variation in conformations of this loop, sparking interest in their further study. The Asgard group, identified as ancestral to eukaryotic PTPs, was successfully expressed and purified under optimized conditions. Current efforts focus on optimizing crystallization to obtain larger crystals for structural analysis. This project will investigate the allosteric regulation of acid and catalytic loops, and the evolution of backup catalytic mechanisms in archaeal PTPs, using computational, kinetic, structural, and spectroscopic approaches and will help us identify common themes that nature decided to preserve.
Location
Logan, UT
Start Date
4-8-2025 11:30 AM
End Date
4-8-2025 12:20 PM
Included in
Biochemistry Commons, Biology Commons, Cell and Developmental Biology Commons, Chemistry Commons
Solving the Structure of an Ancestral Protein Tyrosine Phosphatase
Logan, UT
Protein tyrosine phosphatases (PTPs) regulate cell signaling by removing phosphate groups from tyrosine residues. Malfunction of these enzymes can lead to diseases such as diabetes and cancer. A conserved feature among PTPs is the catalytic acid loop, essential for phosphate removal. Computational analysis of PTP structures revealed that ancestral PTPs have considerable variation in conformations of this loop, sparking interest in their further study. The Asgard group, identified as ancestral to eukaryotic PTPs, was successfully expressed and purified under optimized conditions. Current efforts focus on optimizing crystallization to obtain larger crystals for structural analysis. This project will investigate the allosteric regulation of acid and catalytic loops, and the evolution of backup catalytic mechanisms in archaeal PTPs, using computational, kinetic, structural, and spectroscopic approaches and will help us identify common themes that nature decided to preserve.