6PU0

Pigeon Cryptochrome4 bound to flavin adenine dinucleotide

Summary for 6PU0

• Entry DOI: 10.2210/pdb6pu0/pdb
• Descriptor: Cryptochrome-1, FLAVIN-ADENINE DINUCLEOTIDE, TRIETHYLENE GLYCOL, ... (7 entities in total)
• Functional Keywords: magnetosensor, photolyase, circadian clock protein
• Biological source: Columba livia (Rock dove)
• Total number of polymer chains: 1
• Total formula weight: 59695.73

Authors

Zoltowski, B.D.,Chelliah, Y.,Wickramaratne, A.C.,Jarocha, L.,Karki, N.,Mouritsen, H.,Hore, P.J.,Hibbs, R.E.,Green, C.B.,Takahashi, J.S. (deposition date: 2019-07-16, release date: 2019-09-04, Last modification date: 2023-10-11)

Primary citation

Zoltowski, B.D.,Chelliah, Y.,Wickramaratne, A.,Jarocha, L.,Karki, N.,Xu, W.,Mouritsen, H.,Hore, P.J.,Hibbs, R.E.,Green, C.B.,Takahashi, J.S.
Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon.
Proc.Natl.Acad.Sci.USA, 116:19449-19457, 2019

PubMed 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 (pigeon) CRY4 that reveal evolutionarily conserved modifications to a sequence of Trp residues (Trp-triad) required for CRY photoreduction. In CRY4, 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.

PubMed: 31484780
DOI: 10.1073/pnas.1907875116

Experimental method

X-RAY DIFFRACTION (1.8979 Å)