Audrey
Lamb
Assistant Professor
Molecular Biosciences
The Structural Biology of Pyoverdin Biosynthesis
Mentor:
William
Picking
The main goal of this research is to understand in atomic detail the molecular mechanisms of siderophore production. Siderophores are iron chelators (ligands reversibly bound to metal ions) that are involved in the virulence of pathogenic bacteria, including Pseudomonas aeruginosa, yersinia pestis and Vibrio cholerae. These bacteria cannot survive in the iron-limiting environment of the human host if siderophore production is disrupted. Therefore, structural information about the enzymes required to produce these chemically-related siderophores may provide new antimicrobial targets important in the fight against chronic pneumonia in cystic fibrosis patients (P. aeruginosa), plague (Y. pestis) and cholera (V. cholera). This proposal focuses on the x-ray crystallographic structure determination of three enzymes in pyoverdin biosynthesis by P. Aeruginosa: PvdA, PvdF, and PvdJ.
Dr. Lamb previously was the recipient of a COBRE in Protein Structure and Function Pilot Project Grant (awarded January 2004) for the project "Structural Analysis of Siderophore Biosynthesis."
Copyright © 2006
Center for Biomedical Research Excellence in Protein Structure and Function
Department of Medicinal Chemistry, School of Pharmacy
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