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


Autoria(s): Prescott, M.; Ling, M.; Beddoe, T.; Oakley, A. J.; Dove, S.; Hoegh-Guldberg, O.; Devenish, R. J.; Rossjohn, J.
Contribuinte(s)

Victoria Mountain

Data(s)

01/03/2003

Resumo

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, non-fluorescent pocilloporin to 2.2 Angstrom resolution and a genetically engineered fluorescent variant to 2.4 Angstrom resolution. The pocilloporin chromophore structure adopts a markedly different conformation in comparison with the DsRed chromophore, despite the chromophore sequences (Gin-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.

Identificador

http://espace.library.uq.edu.au/view/UQ:67391

Idioma(s)

eng

Publicador

Cell Press

Palavras-Chave #Biochemistry & Molecular Biology #Biophysics #Cell Biology #Pocilloporin #Pigment #Chromophore #Fluorescence #Green Fluorescent Protein #Dsred #Gfp-like Proteins #Corals #Homolog #Family #C1 #270201 Gene Expression #770403 Living resources (flora and fauna)
Tipo

Journal Article