Smith, Steven P - Queen's University - Department of Biomedical and Molecular Sciences

个人简介

My research program involves the use of structural biology (i.e., nuclear magnetic resonance (NMR), X-ray crystallography, small-angle X-ray scattering), biophysical methods and complementary cell biology appraoches to identify the molecular determinants regulating macromolecular complex assemlby and function. We are currently studying the following systems: 1) mucin-degrading enzymes and enzyme complexes from the opportunistic pathogen Clostridium perfringens 2) the assembly, organization, and higher order structure of the cellulosome, a highly efficient lignocellulose-degrading bacterial enzyme complex, and 3) the molecular determinants of E2A transcriptional factor-target protein inteactions that regulate lymphopoiesis and acute lymphoblastic leukemia.

研究领域

My research program involves the use of structural biology (i.e., nuclear magnetic resonance (NMR), X-ray crystallography, small-angle X-ray scattering), biophysical methods and complementary cell biology approaches to identify the molecular determinants regulating macromolecular complex assembly and function. We are currently studying the following systems: 1) The assembly, organization, and higher order structure of the cellulosome, a highly efficient lignocellulose-degrading bacterial enzyme complex, 2) the molecular basis of transcriptional regulation in health and diesease, including the role of the transcription factor E2A in lymphopoiesis and acute lymphoblastic leukemia.

近期论文

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1. Denis, C.M., Langelaan, D., Kirlin, A.C., Chitayat, S., Munro, K., Spencer, H.L., LeBrun, D.P. & Smith, S.P. (2014) Functional redundancy between the transcriptional activation domains of E2A is mediated by binding to the KIX domain of CBP/p300. Nucleic Acids Res. 42: 7370-7382. 2. Grondin, J., Chitayat, S., Ficko-Blean, E., Boraston, A.B. & Smith, S.P. (2014) An unusual mode of galactose recognition by a family 32 carbohydrate-binding module. J. Mol. Biol. 426: 869-880. 3. Smith, S.P. & Bayer, E.A. (2013) Insights into cellulosome assembling and dynamics: from dissection to reconstruction of the supramolecular enzyme complex. Curr. Opin. Struct. Biol. 23: 686-694. 4. Currie, M.A., Cameron, K., Dias, F.M.V., Spencer, H.L., Bayer, E.A., Fontes, C.M.G.A., Jia, Z., Smith, S.P. (2013) Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure. J. Biol. Chem. 288: 7978-7985. 5. Denis, C.M., Chitayat, S., Plevin, M.J., Wang, F., Thompson, P., Lui, S., Spencer, H.L., Ikura, M., LeBrun, D.P. & Smith, S.P. (2012) Structural basis of CBP/p300 recruitment in leukemia induction by E2A-PBX1. Blood. 120: 3968-3977. 6. Currie, M.A., Adams, J.J., Faucher, F., Bayer, E.A., Jia, Z. & Smith, S.P. (2012) Cellulosomal modular architecture and structural plasticity revealed by ternary complex from the Clostridium thermocellum scaffoldin subunit. J. Biol. Chem. 287: 26953-26961. 7. Adams, J.J., Gregg, K., Bayer, E.A., Boraston, A.B. & Smith, S.P. (2008) Structural basis for a novel mode of Clostridium perfringens toxin complex formation. Proc. Natl. Acad. Sci. USA. 105: 12194-12199.