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George W. and Grace L. Todd Professor of Chemistry, Chemistry
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.
Protein electron transfer reactions, photochemistry, nitric oxide and nitration in biological systems
- Chemistry and Chemical Biology
- Biochemistry, Molecular and Cell Biology
- Chemistry and Chemical Biology
- Tri-Institutional Training Program in Chemical Biology (TPCB)
- Chemical Biology and Experimental Therapeutics Committee
- Weill Institute for Cell and Molecular Biology Advisory Committee
- 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
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.