Faculty Bio
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) 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 interactions that regulate lymphopoiesis and acute lymphoblastic leukemia.
Research Interests
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) 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 interactions that regulate lymphopoiesis and acute lymphoblastic leukemia.
Selected Publications
1. Smith, S.P., Bayer, E.A. & Czjzek, M. (2017) Continually emerging mechanistic complexity of the multi-enzyme celluolsomal complex. Curr. Opin. Struct. Biol. In press.
2. Grondin, J.M., Duan, D., Kirlin, A.C., Chitayat, S., Furness, H.S., Spencer, H.L., Spencer, C., Campigotto, A., Houliston, S., Arrowsmith, C.H., Allingham, J.S., Boraston, A.B. & Smith, S.P. (2017) Carbohydrate recognition by a family 31 glycoside hydrolase from Clostridium perfringens. PLoS One. 12: e0171606.
3. Langelaan, D.N., Liburd, J., Miller, E., Yang, Y., Chitayat, S., Crawley, S.W., Côté, G.P. & Smith, S.P. (2016) Structure of the single-lobe MlcC in complex with the light chain-binding domains of myosin-1C provides insights into divergent IQ-motif recognition. J. Biol. Chem. 291: 19607-19617
4. 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.
5. 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.
6. 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.
7. 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.
8. 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.
9. 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.
10. Adams, J.J., Gregg, K., Bayer, E.A., Boraston, A.B. & Smith, S.P. (2008) Structural basis for a novel mode of Clostridium perfringenstoxin complex formation. Proc. Natl. Acad. Sci. USA. 105: 12194-12199.