Andrew J. Fisher

Andy Fisher

Position Title

Department of Chemistry
Department of Molecular and Cellular Biology

4A Briggs

X-ray crystallography is one of the most powerful tools to examine protein structure at atomic detail. My laboratory uses single crystal x-ray diffraction techniques to determine the three-dimensional structure of biologically important proteins. Knowledge of the atomic resolution structure provides tremendous insight into understanding how the protein functions. Hypotheses on structure - function relationships can be drawn from the crystal structure, which can be tested using crystallography and other biophysical and biochemical techniques. Currently, the laboratory is focusing on enzymes in the biologically important pathways of RNA editing, 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

  • 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.  In Press,

  • 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]

  • Hurlburt, N. K., Chen, L. H., Stergiopoulos, I., and Fisher, A. J. (2018). Structure of the Cladosporium fulvum Avr4 effector in complex with (GlcNAc)6 reveals the ligand-binding mechanism and uncouples its intrinsic function from recognition by the Cf-4 resistance protein. PLoS Pathog. 14(8):e1007263. [PDF Reprint]

  • Fisher, A. J., and Beal, P. A. (2018). Structural basis for eukaryotic mRNA modification. Curr. Opin. Struct. Biol. 53:59-68. [PDF Reprint]

  • McArthur, J. B., Yu, H., Tasnima, N., Lee, C. M., Fisher, A. J., and Chen, X. (2018). α2-6-Neosialidase: A sialyltransferase mutant as a sialyl linkage-specific sialidase. ACS Chemical Biology 13:1228-1234. [PDF Reprint]

  • Lal, N. K., Nagalakshmi, U., Hurlburt, N. K., Flores, R., Bak, A., Sone, P., Ma, X., Song, G., Walley, J., Shan, L., He, P., Casteel, C., Fisher, A. J., Dinesh-Kumar, S. P. (2018). Nuclear role of a plant receptor-like cytoplasmic kinase in hormone regulation during innate immunity. Cell & Host Microbe  23:485-497.  [PDF Reprint]