Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Zoltowski BD,Chelliah Y,Wickramaratne A,Jarocha L,Karki N,Xu W,Mouritsen H,Hore PJ,Hibbs RE,Green CB,Takahashi JSdoi
10.1073/pnas.1907875116subject
Has Abstractpub_date
2019-09-24 00:00:00pages
19449-19457issue
39eissn
0027-8424issn
1091-6490pii
1907875116journal_volume
116pub_type
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