Brian Crane

George W. and Grace L. Todd Professor

336 Physical Science Bldg
bc69@cornell.edu
607/254-8634

Education

PhD, The Scripps Research Institute
BSc, University of Manitoba

Departments and programs

CDER
Chemistry and Chemical Biology

Affiliated Colleges

College of Arts and Sciences

Academic interests

Bioinorganic
Biophysical
Chemical Biology

Keywords

Protein electron transfer reactions, photochemistry, nitric oxide and nitration in biological systems

Overview

The Crane group studies structure, function and mechanism of protein systems that underlie signal transduction. Of particular emphasis are processes mediated by redox and photochemistry and those dependent on highly cooperative macromolecular assemblies. Projects include understanding circadian clock light sensors, bacterial transmembrane signaling, nitric oxide enzymology and general aspects of protein electron transfer.

Research Focus

Understanding interactions among proteins, electrons, and photons
How metalloenzymes stabilize transient intermediates during catalysis
How protein structure controls long-range electron transfer
How photo and redox processes are used in biological information transfer
Combine genetic and chemical manipulation of proteins, atomic-resolution structure determination, and novel photochemically triggered experiments in single crystals
Understanding How Structure Controls Electron Transfer and Activated States in Metalloenzymes
Bacterial Nitric Oxide Synthases:
Light and Redox Sensing
Bacterial Chemotaxis

Publications

Vaidya AT, Chen CH, Dunlap JC, Loros JJ, Crane BR. Structure of a Light-Activated LOV Protein Dimer That Regulates Transcription. Sci Signal. 2011, 4
Paul K, Gonzalez-Bonet G, Bilwes AM, Crane BR, Blair D. Architecture of the flagellar rotor. EMBO J. 2011, 30, 2962-71.
Airola MV, Watts KJ, Bilwes AM, Crane BR. Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure 2010, 18, 436-48.
Bhatnagar J, Borbat PP, Pollard AM, Bilwes AM, Freed JH, Crane BR. Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy. Biochemistry 2010, 49, 3824-41.
Patel BA, Moreau M, Widom J, Chen H, Yin L, Hua Y, Crane BR. Endogenous nitric oxide regulates the recovery of the radiation-resistant bacterium Deinococcus radiodurans from exposure to UV light. Proc Natl Acad Sci U S A 2009, 106, 18183-8.
Zoltowski BD, Vaccaro B, Crane BR. Mechanism-based tuning of a LOV domain photoreceptor. Nat Chem Biol. 2009, 5, 827-34.
Zoltowski, B.D., Schwerdtfeger, C., Widom, J. Loros, J.J., Bilwes, A. M., Dunlap, J., C. & Crane, B.R. Conformational switching in the fungal light sensor Vivid. Science, 2007, 316 1054-1057.
Park, S. Y., Borbat, P. P., Gonzalez-Bonet, G., Bhatnagar, J., Freed, J. H., Bilwes, A. M. & Crane, B. R. Reconstruction of the chemotaxis receptor:kinase assembly. Nat. Struct. Mol. Biol., 2006, 13, 400-407.
Chao, X., Muff, T., Park, S., Zhang, S., Pollard, A. M., Ordal, G., Bilwes, A. M. & Crane, B.R. A receptor-modifying deamidase in complex with a signaling phosphatase reveals a mechanism of reciprocal regulation. Cell, 2006, 124, 561-571.
Kang, S. A. & Crane, B.R. Effects of interface mutations on association modes and electron transfer rates between proteins. Proc. Natl. Acad. Sci. USA, 2005, 102, 15465-15470.
Kers, J. A., Wach, M. J., Krasnoff, S. B., Widom, J., Cameron, K. D., Bukhalid, R. A., Gibson, D. M., Crane, B. R. & Loria, R. Nitration of a peptide phytotoxin by bacterial nitric oxide synthase. Nature, 2004, 429, 79-82.