dd
Andrew J. Fisher
Professor

Email: fisher@chem.ucdavis.edu
Phone:(530) 754-6180
Fax:(530) 752-8995

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

Group Page
Principal Research Interests
Warning: fclose(): supplied argument is not a valid stream resource in /var/www/html/faculty/cf-info.php on line 238
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; sulfate activation, sialic acid transfer, and chromophore biosynthesis.
Representative Publications

Ni, L., Chokhawala, H., Cao, H., Henning, R., Ng, L., Huang, S., Yu, H., Chen, X., and Fisher, A. J. (2007). Crystal structures of Pasteurella multocida sialyltransferase complexes with acceptor and donor analogs reveal substrate binding sites and catalytic mechanism. Biochemistry46:6288-6298.

Tu, S.-L, Rockwell, N. C., Lagarias, J. C., and Fisher, A. J. (2007). Insight into the radical mechanism of phycocyanobilin:ferredoxin oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical measurements. Biochemistry 46:1484-1494.

Yu, Z., Lansdon, E. B., Segel, I. H., and Fisher, A.J. (2007). Crystal structure of the Bi-functional ATP Sulfurylase/APS kinase from Chemolithotrophic Thermophile Aquifex aeolicus. J. Mol. Biol. 365:732-743.

Ni, L., Sun, M., Yu, H., Chokhawala, H., Chen, X., and Fisher, A. J. (2006). Cytidine 5'-Monophosphate (CMP)-Induced Structural Changes in a Multifunctional Sialyltransferase from Pasteurella multocida. Biochemistry 45:2139-2148.

Fisher, A. J., MacRae, I. J., Beynon, J. D., Lansdon, E. B., and Segel, I. H. (2004). Optimizing an enzyme for its physiological role: Structural and functional comparisons of ATP sulfurylases from three different organisms. In: Conformational Proteomics of Macromolecular Architecture. Cheng, R. H., and Hammar, L. (Eds.) World Scientific Publishing Co., London. p. 222-241.

Lansdon, E. B., Fisher, A. J., and Segel, I. H. (2004). Human PAPS Synthetase (Isoform 1; Brain): Kinetic Properties of the ATP Sulfurylase and APS Kinase Domains. Biochemistry 43:4356-4365.Forsyth, C., M., Lemongello, D., LaCount, D. J., Friesen, P. D., and Fisher, A. J. (2004). Crystal Structure of an Invertebrate Caspase. J. Biol. Chem. 279:7001-7008.

Corneillie, T. M., Fisher, A. J., and Meares, C. F. (2003). Crystal Structure of Two Complexes of the Rare Earth-DOTA-Binding Antibody 2D12.5: Ligand Generality from a Chiral System. J. Am. Chem. Soc. 125:15039-15048.

MacRae, I. J., Segel, I. H., and Fisher, A. J.(2002). Allosteric Inhibition via R-State Destabilization in ATP Sulfurylase from P. chrysogenum.Nature Struc. Biol9:945-949.

Lansdon, E. B., Segel, I. H., and Fisher, A. J. (2002). Ligand-Induced Structural Changes in Adenosine 5´-Phosphosulfate Kinase from Penicillium chrysogenum.Biochemistry 41:13672-13680.