The 2.2 A crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation |
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Authors: | Prescott Mark Ling Michael Beddoe Travis Oakley Aaron J Dove Sophie Hoegh-Guldberg Ove Devenish Rodney J Rossjohn Jamie |
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Affiliation: | Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, 3800, Victoria, Australia. mark.prescott@med.monash.au |
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Abstract: | 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 A resolution and a genetically engineered fluorescent variant to 2.4 A 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. |
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