Date of Award


Document Type

Open Access Thesis


Chemistry and Biochemistry


College of Arts and Sciences

First Advisor

Maksymilian Chruszcz


Vibrio vulnificus, a gram-negative bacterium, is the leading cause of seafood-borne illnesses and mortality in the United States. Previous studies of bacterial pathogens have identified a metabolite essential to V. vulnificus growth and function. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (Dxr) is an essential enzyme in the viability of many bacteria and catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (Dxp) to 2-C-methylerythritol 4-phosphate (MEP) within the MEP pathway found in plants and bacteria. Previous studies have been conducted to characterize Dxr homologs from other pathogens including E. coli, M. tuberculosis, and P. falciparum. Information on the structural and enzymatic characteristics of Dxr from Vibrio vulnificus, or VvDxr, is not known. In this study, we show for the first time apo and ligand-bound structures of VvDxr. The structures are from both His-tag cleaved (cut) and uncleaved (uncut) protein. Using Dxr homologs, we identify similarities in the structural characteristics among these enzymes. The binding characteristics were also studied to identify parallels between the enzyme’s affinity for metals and inhibitors. Our findings will provide basis for design of Dxr inhibitors that may find application as antimicrobial compounds.

Included in

Chemistry Commons