Reef-building corals contain host pigments, termed pocilloporins, that function to regulate the light environment of their resident microalgae by acting as a photoprotectant in excessive sunlight. We have determined the crystal structure of an intensely blue, nonfluorescent pocilloporin to 2.2 Å resolution and a genetically engineered fluorescent variant to 2.4 Å resolution. The pocilloporin chromophore structure adopts a markedly different conformation in comparison with the DsRed chromophore, despite the chromophore sequences (Gln-Tyr-Gly) being identical; the tyrosine ring of the pocilloporin chromophore is noncoplanar and in the trans configuration. Furthermore, the fluorescent variant adopted a noncoplanar chromophore conformation. The data presented here demonstrates that the conformation of the chromophore is highly dependent on its immediate environment.
CITATION STYLE
Prescott, M., Ling, M., Beddoe, T., Oakley, A. J., Dove, S., Hoegh-Guldberg, O., … Rossjohn, J. (2003). The 2.2 Å crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation. Structure, 11(3), 275–284. https://doi.org/10.1016/S0969-2126(03)00028-5
Mendeley helps you to discover research relevant for your work.