6PU0

Pigeon Cryptochrome4 bound to flavin adenine dinucleotide

6PU0 の概要

• エントリーDOI: 10.2210/pdb6pu0/pdb
• 分子名称: Cryptochrome-1, FLAVIN-ADENINE DINUCLEOTIDE, TRIETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: magnetosensor, photolyase, circadian clock protein
• 由来する生物種: Columba livia (Rock dove)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59695.73

構造登録者

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. (登録日: 2019-07-16, 公開日: 2019-09-04, 最終更新日: 2023-10-11)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8979 Å)