Oriana Fisher

Assistant Professor
(610) 758-6259
Seeley G. Mudd, Room 692
Research Interests: 
Biochemistry
Structural biology
Bioinorganic chemistry
Bacterial copper homeostasis
Teaching Interests: 
Biochemistry
Bioinorganic Chemistry
Protein structure and function

Our research group is broadly interested in elucidating the structure and function of bacterial metalloproteins and enzymes, particularly those found in human pathogens. We do this using a number of complementary approaches including X-ray crystallography, biochemistry, biophysics, bioinorganic chemistry, and bioinformatics. One primary research area aims to identify and determine the mechanisms by which previously uninvestigated classes of proteins bind to and transport copper. A second research direction focuses on investigating how enzymes involved in stress-activated signaling pathways can be selectively targeted by antimicrobials.

Selected Recent Publications:

Ross, M.O.*, Fisher, O.S.*, Morgada, M.N., Krzyaniak, M.D., Wasielewski, M., Vila, A.J., Hoffman, B.M., Rosenzweig, A.C. Formation and electronic structure of an atypical CuA site. 2019. J Am Chem Soc. 141, 4678-4686.

Fisher, O.S., Kenney, G.E., Ross, M.O., Ro, S.Y., Lemma, B.E., Batelu, S., Thomas, P.M., Sosnowski, V.C., DeHart, C.J., Kelleher, N.L., Stemmler, T.L., Hoffman, B.M., Rosenzweig, A.C. Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria. 2018. Nat Commun. 9, 4276.

Fisher, O. S.*, Deng, H.*, Liu, D.*, Zhang, Y., Wei, R., Deng, Y. Zhang, F., Louvi, A., Turk, B.E., Boggon, T.J., Su, B. Structure and vascular function of MEKK3-cerebral cavernous malformations complex. 2015. Nat Commun6, 7937.

Draheim, K.M.*, Li, X.*, Zhang, R., Fisher, O.S., Villari, G., Calderwood, D.A., Boggon, T.J. Structural determinants of a CCM3:CCM2 interaction that stabilizes protein expression and permits endothelial network formation. 2015. J Cell Biol. 208, 987-1001.

Fisher, O.S., Liu, W., Zhang, R., Stiegler, A.L., Ghedia, S., Weber, J.L., Boggon, T.J. Structural basis for the disruption of the Cerebral Cavernous Malformations 2 (CCM2) interaction with Krev Interaction Trapped 1 (KRIT1) by disease-associated mutations. 2015. J Biol Chem. 290, 2842-53.

Fisher, O.S. and Boggon, T.J. Signaling pathways and the cerebral cavernous malformations proteins: lessons from structural biology. 2014. Cell Mol Life Sci 71, 1881-1892.

Draheim, K.M., Fisher, O.S., Boggon, T.J., and Calderwood, D.A. Cerebral cavernous malformation proteins at a glance. 2014. J Cell Sci 127, 701-707.

Fisher, O.S., Zhang, R., Li, X., Murphy, J.W., Demeler, B., and Boggon, T.J. Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. 2013. FEBS Lett 587, 272-277.