Todd Yeates earned his PhD at UCLA developing X-ray crystallographic methods while working on early structures of membrane proteins, followed by postdoctoral research at the Scripps Research Institute elucidating the structures of viral capsids. Yeates joined the faculty at UCLA, where his research combines interests in molecular biology, biophysics and computational methods, applied to problems from molecular structure to genomic sequence analysis. Current studies emphasize large protein assemblies, including those found in nature and those that can be created in the laboratory by design. Research in the Yeates group laid out a structural understanding of protein-based metabolic organelles in bacteria, often called 'bacterial microcompartments'. On the design side, the Yeates group developed the first methods for designing highly symmetric self-assembling protein materials, such cubic cages, which are now finding applications in biomedicine, imaging, and biomaterials design.
Research in the Yeates group focuses on a deep understanding of protein structures and large assemblies, with an emphasis on the underlying principles that guide their behavior and evolution, and which enable the atomic level design of novel self-assembling protein architectures.
Our studies of natural self-assembling protein architectures have focused on a remarkable but still not well-appreciated family of giant protein capsids inside many bacterial cells. Our structural studies on the carboxysome and related bacterial microcompartments laid out a mechanistic understanding for these extraordinary structures, showing that bacteria do possess true organelles.
In our frontier bioengineering studies, we are designing entirely novel protein architectures, including cubic cages and extended crystalline arrays in two and three dimensions. Various types of protein assemblies, natural and designed, are finding applications as active enzymatic materials, imaging scaffolds, and biotherapeutics.
McConnell, S.A., Cannon, K.A., Morgan, C., McAllister, R., Amer, B.R., Clubb, R.T., and Yeates, T.O. 2020. Designed protein cages as scaffolds for building multi-enzyme materials. ACS Synth Biol. 9, 381-391.
Liu, Y., Huynh, D.T., Yeates, T.O. 2019. A 3.8 Å resolution cryo-EM structure of a small protein bound to an imaging scaffold. Nat. Commun. 10:1864. doi:10.1038/s41467-019-09836-0.
Cannon, K.A., Ochoa, J.M., Yeates, T.O. 2019. High-symmetry protein assemblies: patterns and emerging applications. Curr. Opin. Struct. Biol. 55, 77-84.
Liu, Y., Gonen, S., Gonen, S., Yeates, T.O. 2018. Near-atomic cryo-EM imaging of a small protein displayed on a designed scaffolding system. PNAS 115, 3362-7.
Lai, Y.-T., Reading, E., Hura, G.L., Tsai, K.L., Laganowsky, A., Asturias, F.J., Tainer, J.A., Robinson, C.V., Yeates, T.O. 2014. Structure of a designed protein cage that self-assembles into a highly porous cube. Nat Chem. 6, 1065-71.
Lai, Y.-T., Cascio, D., Yeates, T.O. 2012. Structure of a 16-nm cage designed by using protein oligomers. Science 336, 1129.
King, N.P., Sheffler, W., Sawaya, M.R., Vollmar, B.S., Sumida, J.P., André, I., Gonen, T., Yeates, T.O., Baker, D. 2012. Computational design of self-assembling protein nanomaterial with atomic level accuracy. Science 336,1171-4.
Tanaka, S., Sawaya, M.R., and Yeates, T.O. 2010. Structure and mechanisms of a protein-based organelle in Escherichia coli. Science 327, 81-4.
Tanaka, S., Kerfeld, C.A., Sawaya, M.R., Cai, F., Heinhorst, S., Cannon, G.C. and Yeates, T.O. 2008. Atomic-level models of the bacterial carboxysome shell. Science 319, 1083-6.
Kerfeld, C.A., Sawaya, M.R., Tanaka, S., Nguyen, C.V., Phillips, M., Beeby, M., and Yeates, T.O. 2005. Protein structures forming the shell of primitive bacterial organelles. Science 309, 936-8.