个人简介

After earning his Bachelor's degree at UCLA, Yeates stayed on to do his PhD research under the direction of Prof. Douglas Rees. There he helped determine the crystal structure of the bacterial photosynthetic reaction center as part of a team racing to determine the first crystal structures of membrane proteins. He then moved to The Scripps Research Institute to do his postdoctoral research on the structure of poliovirus with Prof. James Hogle. Yeates returned to UCLA in 1990 to join the Faculty in the Department of Chemistry and Biochemistry. His interdisciplinary research, combining molecular biology with computing and mathematics, has focused on macromolecular structure and computational genomics. His research findings include: an explanation for why proteins crystallize in certain favored arrangements, the discovery of thermophilic microbes rich in intracellular disulfide bonds, co-development of phylogenetic profile methods in genomics, development of designed protein cages or 'nanohedra', the discovery of novel topological features such as slipknots in thermostable proteins, and the elucidation of the structures of the carboxysome shell proteins. Yeates is a member of the Molecular Biology Institute, the California Nanosystems Institute, the Institute of Genomics and Proteomics, and a Fellow of the American Association for the Advancement of Science. He has published approximately 100 research papers.

研究领域

Biochemistry/Biophysics/Structural and Computational Biology/Bioenergy and the Environment/Theory

Our research covers the areas of molecular, structural and computational biology. In the area of structural biology, our emphasis is on supra-molecular protein assemblies. Much of our recent work has focused on bacterial microcompartments -- extraordinary protein assemblies comprised of thousands of subunits reminiscent of viral capsids. They encapsulate a series of enzymes within a protein shell, which controls the transport of substrates and products into and out of the microcompartment interior. They serve as primitive metabolic organelles in many bacteria. Our structural studies on these systems provided the first three-dimensional views of the shell proteins, and have generated long-needed mechanistic hypotheses for how bacterial microcompartments function.

近期论文

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Yeates TO, Kent SB. (2012). Racemic protein crystallography. Annu Rev Biophys. 2012. 41:41-61. [Abstract] Sawaya MR, Pentelute BL, Kent SB, Yeates TO. (2012). Single-wavelength phasing strategy for quasi-racemic protein crystal diffraction data. Acta Crystallogr. D Biol. Crystallogr.. Jan 2012. 68(Pt 1):62-8. [Abstract] Johnson E, Nguyen PT, Yeates TO, Rees DC. (2012). Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition. Protein Sci.. Jan 2012. 21(1):84-96. [Abstract] Jones EY, Yeates TO. (2012). Structure and function in complex macromolecular assemblies: some evolutionary themes. Curr. Opin. Struct. Biol.. Apr 2012. 22(2):197-9. [Abstract] King NP, Sheffler W, Sawaya MR, Vollmar BS, Sumida JP, André I, Gonen T, Yeates TO, Baker D. (2012). Computational design of self-assembling protein nanomaterials with atomic level accuracy. Science. Jun 2012. 336(6085):1171-4. [Abstract] Lai YT, Cascio D, Yeates TO. (2012). Structure of a 16-nm cage designed by using protein oligomers. Science. Jun 2012. 336(6085):1129. [Abstract]