David K. Wilson

David Wilson

Position Title

  • Molecular and Cellular Biology
03 Briggs Hall

Research Interests

Structural biology of enzymes and protein-protein interactions. Projects include 1) protein engineering of enzymes involved in a xylose assimilation (XXX) pathway 2) structure- and combinatorial-based drug design targetting apicomplexan parasitic infection and 3) characterizing the structure and function of WD-repeat domains in protein-protein interaction. Our primary research tool is x-ray crystallography but we usually complement this with biochemical and genetic experiments.

Education and Degree(s)
  • 1991 B.A. in Biochemistry, Rice University
  • 1996 Ph.D. in Biochemistry, Baylor College of Medicine
  • Mak WS, Wang XK, Arenas R, Cui Y, Bertolani S, Deng WQ, Tagkopoulos I, Wilson DK, Siegel JB (2020) Discovery, Design, and Structural Characterization of Alkane-Producing Enzymes across the Ferritin-like Superfamily. Biochemistry 59:3834-3843.
  • Tabares-da Rosa S, Wogulis LA, Wogulis MD, Gonzalez-Sapienza G, Wilson, DK. Structure and specificity of several triclocarban-binding single domain camelid antibody fragments (2018) J. Mol. Recognit. e2755
  • Stoisser T, Brunsteiner M, Wilson DK, Nidetzky B (2016) Conformational flexibility related to enzyme activity: evidence for a dynamic active-site gatekeeper function of Tyr215 in Aerococcus viridans lactate oxidase. Sci. Rep. 6:27892.
  • Stoisser T, Klimacek M, Wilson DK, Nidetzky B (2015) Speeding up product release: a second-sphere contribution from Tyr191 to the reactivity of L-lactate oxidase revealed in crystallographic and kinetic studies of site-directed mutants FEBS J 282:4130-4140.
  • Stoisser T, Rainer D, Leitgeb S, Wilson DK, Nidetzky B. (2014). The Ala95-to-Gly substitution in Aerococcus viridans L-lactate oxidase revisited - structural consequences at the catalytic site and effect on reactivity with O2 and other electron acceptors. FEBS J. 282:562-578.