个人简介

1996 PhD Biochemistry Baylor College of Medicine 1991 BA Biochemistry Rice University

研究领域

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.

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.

近期论文

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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. Yamamoto K, Wilson DK (2013) Identification, characterization and crystal structure of an aldo-keto reductase (AKR2E4) from the silkworm Bombyx mori with 3-dehydroecdysone reductase activity. Arch. Biochem. Biophys. 538:156-163. di Luccio E, Ishida Y, Leal WS, Wilson DK (2012) Crystallographic observation of pH-induced conformational changes in the Amyelois transitella pheromone-binding protein AtraPBP1. PloS ONE, 8(2). Kamita SG, Wogulis MD, Law CS, Morisseau C, Tanaka H, Huang H, Wilson DK, Hammock BD. (2010) Function of Phenylalanine 259 and Threonine 314 within the Substrate Binding Pocket of the Juvenile Hormone Esterase of Manduca sexta. Biochemistry 49:3733-3742. di Luccio E, Wilson DK. (2008) Comprehensive X-ray structural studies of the quinolinate phosphoribosyl transferase (BNA6) from S. cerevisiae. Biochemistry 47:4039-4050. Wogulis M, Chew E, Donohoue P, Wilson DK. (2008) Identification of formyl kynurenine formamidase and kynurenine aminotransferase from S. cerevisiae using crystallographic, bioinformatic and biochemical evidence Biochemistry 47:1608-1621 di Luccio E, Petschacher B, Voegtli J, Chou HT, Stahlberg H, Nidetzky B, Wilson DK. (2007) Structural and kinetic studies of induced fit in xylulose kinase from E. coli. J. Mol. Biol. 365:783-798. di Luccio E, Elling RA, Wilson DK. (2006) Identification of a novel NADH-specific aldo-keto reductase using sequence and structural homologies. Biochem. J. 400:105-114 Ehrensberger AH, Elling RA, Wilson DK. (2006) Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity. Structure 14:567-575. Wogulis M, Wheelock CE, Kamita SG, Hinton AC, Whetstone PA, Hammock BD, Wilson DK. (2006) Structural studies of a potent insect maturation inhibitor bound to the juvenile hormone esterase of Manduca sexta. Biochemistry 45:4045-4057. Cerna D, Wilson DK. (2005) The structure of Sif2p, a WD protein functioning in the SET3 corepressor complex. J. Mol. Biol. 351:923-935. Wogulis MD, Morgan, T, Ishida Y, Leal WS, Wilson DK. (2005) The crystal structure of an odorant binding protein from Anopheles gambiae: evidence for a common ligand release mechanism. Biochem. Biophys. Res. Com. 339:157-164. Wilson DK, Cerna D, Chew E. (2005) The 1.1 Ã… structure of the spindle checkpoint protein Bub3p reveals functional regions. J. Biol. Chem. 280:13944-13951. Dixon S, Robins L, Elling RA, Liu R, Lam KS, Wilson DK, Kurth MJ. (2005) Discovery of selective aldo-keto reductase ligands: an on-bead assay strategy. Bioorg. Med. Chem. Letts. 15:2938-2942.