Honors College Thesis

 

The Crystal Structure of the Potential Drug Target Mycoplasma pneumoniae Glycerol 3-Phosphate Oxidase Public

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  • Mycoplasma pneumoniae is the primary cause of community-acquired pneumonias, including what is commonly known as walking pneumonia. This disease affects people from all demographics, but especially children and older adults. Outbreaks are a significant public health concern and work to develop new pharmacological agents is currently being researched. How M. pneumoniae causes disease is not fully understood, but studies have pointed to hydrogen peroxide as a pathogenicity factor. It is produced as a byproduct of glycerol metabolism by the enzyme glycerol 3-phosphate oxidase (GlpO). Using X-ray crystallography, we determined the three-dimensional structure of this enzyme in order to elucidate its binding properties and guide structure-based drug design efforts. Here, we report the crystallization of M. pneumoniae GlpO along with the native structures of oxidized and reduced GlpO at resolutions of to 2.4 Å and 2.5 Å, respectively. We compared GlpO from M. pneumoniae to another GlpO, a glycerol 3-phosphate dehydrogenase, a glycine oxidase, and the most structurally similar protein which is a protein of an unknown function from Bordetella pertussis.
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