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The 2.2 �� crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation

Journal Article


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 �� resolution and a genetically engineered fluorescent variant to 2.4 �� 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.

Publication Date


  • 2003

Citation


  • Prescott, M., Ling, M., Beddoe, T., Oakley, A. J., Dove, S., Hoegh-Guldberg, O., . . . Rossjohn, J. (2003). The 2.2 �� crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation. Structure, 11(3), 275-284. doi:10.1016/S0969-2126(03)00028-5

Scopus Eid


  • 2-s2.0-0141749127

Start Page


  • 275

End Page


  • 284

Volume


  • 11

Issue


  • 3

Place Of Publication


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 �� resolution and a genetically engineered fluorescent variant to 2.4 �� 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.

Publication Date


  • 2003

Citation


  • Prescott, M., Ling, M., Beddoe, T., Oakley, A. J., Dove, S., Hoegh-Guldberg, O., . . . Rossjohn, J. (2003). The 2.2 �� crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation. Structure, 11(3), 275-284. doi:10.1016/S0969-2126(03)00028-5

Scopus Eid


  • 2-s2.0-0141749127

Start Page


  • 275

End Page


  • 284

Volume


  • 11

Issue


  • 3

Place Of Publication