Protozoa of the genus Plasmodium are responsible for malaria, perhaps the most important parasitic disease to inflect mankind. The emergence of Plasmodium strains resistant to current therapeutics and prophylactics makes the development of new treatment strategies urgent. Among the potential targets for new antimalarial drugs is the BolA-like protein PFE0790c (Pf-BolA). While the function of BolA is unknown, it has been linked to cell morphology by regulating transcription in response to stress. The solution structure for Pf-BolA was determined using NMR-based based and an ensemble of 20 structures deposited into the PDB (2KDN). The overall topology of the Pf-BolA structure, a1-ß1-ß2-a2-a3-ß3-a4 with a mixed ß-sheet, is similar the fold observed in other BolA structures. A helix-turn-helix motif similar to the class II KH fold associated with nucleic acid binding proteins is present, but, contains a FXGXXXL signature sequence different from the GXXG signature sequence present in class II KH folds, suggesting the BolA family of proteins may use a novel protein-nucleic acid interface. A well-conserved arginine residue, R50, hypothesized to play a role in governing the formation of the C-terminal a-helix in the BolA family of proteins is too distant to form polar contacts with any side chains in this a-helix in Pf-BolA suggesting that this conserved arginine may only serve a role in guiding the orientation of this C-terminal helix in some BolA protein. A survey of BolA structures suggests that the C-terminal helix may not have a functional role and a-helix-3 has a “kink” that appears to be conserved among the BolA protein structures. Circular dichroism spectroscopy shows Pf-BolA is fairly robust, partially unfolding when heated to 353 K and refolding upon cooling to 298 K.