Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon

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 vertebr...

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Main Authors: Zoltowski, B, Chelliah, Y, Wickramaratne, A, Jarocha, L, Karki, N, Xu, W, Mouritsen, H, Hore, P, Hibbs, R, Green, C, Takahashi, J
Format: Journal article
Language:English
Published: National Academy of Sciences 2019
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author Zoltowski, B
Chelliah, Y
Wickramaratne, A
Jarocha, L
Karki, N
Xu, W
Mouritsen, H
Hore, P
Hibbs, R
Green, C
Takahashi, J
author_facet Zoltowski, B
Chelliah, Y
Wickramaratne, A
Jarocha, L
Karki, N
Xu, W
Mouritsen, H
Hore, P
Hibbs, R
Green, C
Takahashi, J
author_sort Zoltowski, B
collection OXFORD
description 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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spelling oxford-uuid:88a1da24-b2df-42dd-9f61-f7f7f9d1f4742022-03-26T22:18:46ZChemical and structural analysis of a photoactive vertebrate cryptochrome from pigeonJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:88a1da24-b2df-42dd-9f61-f7f7f9d1f474EnglishSymplectic Elements at OxfordNational Academy of Sciences2019Zoltowski, BChelliah, YWickramaratne, AJarocha, LKarki, NXu, WMouritsen, HHore, PHibbs, RGreen, CTakahashi, JComputational 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.
spellingShingle Zoltowski, B
Chelliah, Y
Wickramaratne, A
Jarocha, L
Karki, N
Xu, W
Mouritsen, H
Hore, P
Hibbs, R
Green, C
Takahashi, J
Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon
title Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon
title_full Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon
title_fullStr Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon
title_full_unstemmed Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon
title_short Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon
title_sort chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon
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