6pu0

Pigeon Cryptochrome4 bound to flavin adenine dinucleotidePigeon Cryptochrome4 bound to flavin adenine dinucleotide

Structural highlights 6pu0 is a 1 chain structure with sequence from Columba livia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8979Å Ligands: , , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2I0LZR8_COLLI Publication Abstract from PubMed 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. Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon.,Zoltowski BD, Chelliah Y, Wickramaratne A, Jarocha L, Karki N, Xu W, Mouritsen H, Hore PJ, Hibbs RE, Green CB, Takahashi JS Proc Natl Acad Sci U S A. 2019 Sep 24;116(39):19449-19457. doi:, 10.1073/pnas.1907875116. Epub 2019 Sep 4. PMID:31484780 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cryptochrome 3D structures

spinqualitylabelsall models 6pu0, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image