Andrew J. Fisher

Andy Fisher

Professor

  • Department of Chemistry
  • Department of Molecular and Cellular Biology
4A Briggs

Our laboratory is interested in the relationships between structure and function of biologically important macromolecules.  The lab utilizes the disciplines of X-ray crystallography and Cryo-EM to determine the atomic resolution structures of the macromolecules and higher-ordered complexes. The molecule’s atomic resolution structure provides tremendous insight into understanding how the macromolecule functions. Hypotheses on structure – function relationships can be drawn from the structures, which are investigated using biochemistry, cell biology, and other biophysical techniques. Currently, the laboratory is focusing on three important biochemical pathways; RNA editing by ADARs, sulfate activation, and glycobiology.

Education, Research and Professional Highlights

  • Appointed to UC Davis Molecular and Cellular Biology faculty (1996)
  • Appointed to UC Davis Department of Chemistry faculty (1996)
  • NIH Postdoctoral fellow, University of Wisconsin-Madison (1992-1996)
  • Linus Pauling Prize, American Crystallographic Association (1991)
  • Ph.D. Biophysics, Purdue University (1992)
  • B.S. Biochemistry, Purdue University (1987)

Recent Publications

  • Doherty, E., Karki, A., Wilcox, X., Mendoza, H., Manjunath, A., Jauregui-Matos, V., Fisher, A. J., and Beal, P. A. (2022). ADAR Activation by Inducing a Syn Conformation at Guanosine Adjacent to an Editing Site. Nucleic Acids Res., 50:10857-10868.

  • Liu, L., Wilcox, X., Fisher, A. J., Boyd, S. D., Zhi, J., Winkler, D. D., Bulla, L. A.  (2022). Functional and Structural Analysis of the Toxin-Binding Site of the Cadherin G‑Protein-Coupled Receptor, BT‑R1, for Cry1A Toxins of Bacillus thuringiensis. Biochemistry, 61:752-766.

  • Doherty, E., Wilcox, X., van Sint Fiet, L., Kemmel, C., Turunen, J., Klein, B., Tantillo, D., Fisher, A. J., and Beal, P. A. (2021). Rational Design of RNA Editing Guide Strands: Cytidine Analogs at the Orphan Position. J. Am. Chem. Soc., 143:6865-6876.

  • Yu, Q., Anderson, D. E., Kaur, R., Fisher, A. J., and Ames, J. B. (2021). Crystal Structure of Calmodulin Bound to the Cardiac Ryanodine Receptor (RyR2) at Residues: Phe4246 to Val4271, Reveals a Fifth Calcium Binding Site. Biochemistry, 60:1088–1096.

  • Unger, E. K., Keller, J. P., Altermatt, M., Liang, R., Matsui, A., Dong, C., Hon, O. J., Yao, Z., Sun, J., Banala, S., Flanigan, M. E., Jaffe, D. A., Hartanto, S., Carlen, J., Mizuno, G. O., Borden, P. M., Shivange, A. V., Cameron, L. P., Sinning, S., Underhill, S. M., Olson, D. E., Amara, S. G., Temple Lang, D., Rudnick, G., Marvin, J. S., Lavis, L. D., Lester, H. A., Alvarez, V. A., Fisher, A. J., Prescher, J. A., Kash, T. L., Yarov-Yarovoy, V., Gradinaru, V., Looger, L. L., and Tian, L. (2020). Directed Evolution of a Selective and Sensitive Serotonin Sensor via Machine Learning.  Cell.   183:1986-2002

  • Moreno, M. V., Rockwell, N. C., Mora, M., Fisher, A. J., and Lagarias, J. C. (2020). A far-red cyanobacteriochrome lineage specific for verdins. Proc. Natl. Acad. Sci. U.S.A., 117:27962-27970.

  • Hurlburt, N. K., Guan, J., Ong, H., Yu, H., Chen, X., and Fisher, A. J. (2020). Structural characterization of a non-hydrolyzing UDP-GlcNAc 2-epimerase from Neisseria meningitidis serogroup A. Acta Crystallogr. F Struct. Biol. Commun. 76:557-567.

  • Feng, Y., Hua, X., Shen, Q., Matthews, M., Zhang, Y., Fisher, A. J., Lyu, X., and Yang, R. (2020) Insight into the potential factors influencing the catalytic direction in cellobiose 2-epimerase by crystallization and mutagenesis, Acta Crystallogr. D Struct. Biol. 76:1104-1113.

  • Thuy-Boun, A. S., Thomas, J. M., Grajo, H. L., Palumbo, C. M., Park, S., Nguyen, L. T., Fisher, A. J., and Beal, P. A. (2020). Asymmetric Dimerization of Adenosine Deaminase acting on RNA Facilitates Substrate Recognition. Nucleic Acids Res.  48:7958-7972.

  • Matthews, M. M., McArthur, J. B., Li, Y., Yu, H., Chen, X., Fisher, A. J. (2020). Catalytic cycle of Neisseria meningitidis CMP-sialic acid synthetase illustrated by high-resolution protein crystallography. Biochemistry 59:3157-3168.

  • Li, Y., Li, R., Yu, H., Sheng, X., Wang, J., Fisher, A. J., Chen, X. (2020). Enterococcus faecalis α1–2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification. FEBS Letters 594:439-451. [PDF Reprint]

  • Monteleone, L. R., Matthews, M. M., Palumbo, C. M., Thomas, J. M., Zheng, Y., Chiang, Y, Fisher, A., J., and Beal, P. A. (2019). A bump-hole approach for directed RNA editing. Cell Chem. Biol. 26:269-277. [PDF Reprint]

Tags

Biophysical Chemical Biology