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Structural Studies of DsbA and its Putative Partner, VKOR, in Mycobacterium tuberculosis Katie P. Nguyen Mentor: Celia Goulding Disulfide bond-forming (Dsb) proteins are essential for the correct folding and disulfide bond formation of secreted proteins. In Mycobacterium tuberculosis, DsbA is proposed to be a disulfide isomerase and is believed to be re-oxidized by its putative partner, vitamin K epoxide reductase (VKOR). The intent of this study is to further investigate the molecular determinants of the interactions between DsbA and VKOR by X-ray crystallography. In order to achieve this, DsbA crystals were grown in order to be soaked with a VKOR heptapeptide that binds with an apparent KD of 2.9 µM. Cocrystallization screens of DsbA and the VKOR heptapeptide were set up and crystals were obtained. The cloning and protein overexpression of two different constructs of DsbA-VKOR fusion proteins was performed. I was able to successfully obtain crystals for DsbA alone and for the cocrystallization of DsbA with the VKOR heptapeptide. In addition, we believe that the DsbA-VKOR fusion protein was successfully overexpressed in a condition that resembles the overexpression conditions of full-length VKOR in Synechococcus sp.