Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 116, Issue 39, Pages 19449-19457Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1907875116
Keywords
magnetoreception; cryptochromes; photobiology
Categories
Funding
- NSF [MCB-1613643]
- NIH [NS095899, DA042072, R01 GM090247, R01 GM112991, R35 GM127122]
- Deutsche Forschungsgemeinschaft [SFB 1372, GRK 1885]
- Air Force Office of Scientific Research (Air Force Materiel Command, USAF Award) [FA9550-14-1-0095]
- European Research Council (European Union's 7th Framework Programme, FP7/20072013/ERC Grant) [340451]
- European Research Council (Horizon 2020 research and innovation program, ERC Synergy Grant) [810002]
- NIH, National Institute of General Medical Sciences [P30 GM124165]
- NIH Office of Research Infrastructure Programs High-End Instrumentation Grant [S10 RR029205]
- DOE Office of Science [DE-AC02-06CH11357]
- HHMI
- Office of Science, Office of Basic Energy Sciences of the US Department of Energy [DE-AC02-05CH11231]
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Computational and biochemical studies implicate the blue-light sensor cryptochrome (CRY) as an endogenous light-dependent magnetosensor enabling migratory birds to navigate using the Earth's magnetic field. Validation of such a mechanism has been hampered by the absence of structures of vertebrate CRYs that have functional photochemistry. Here we present crystal structures of Columba livia (pigeon) CRY4 that reveal evolutionarily conserved modifications to a sequence of Trp residues (Trp-triad) required for CRY photoreduction. In ClCRY4, the Trp-triad chain is extended to include a fourth Trp (W369) and a Tyr (Y319) residue at the protein surface that imparts an unusually high quantum yield of photoreduction. These results are consistent with observations of night migratory behavior in animals at low light levels and could have implications for photochemical pathways allowing magnetosensing.
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