Structural-functional analysis of the oligomeric protein R-phycoerythrin
The structure of phycobiliproteins and their spatial organization in the phycobilisome provide the environment for high efficiency in light harvesting and conduction towards photosystem II. This article focuses on the analysis of R-phycoerythrin, a light harvesting hexameric phycobiliprotein that is...
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| Autores principales: | , , , |
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| Lenguaje: | English |
| Publicado: |
Sociedad de Biología de Chile
2004
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| Materias: | |
| Acceso en línea: | http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000500003 |
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| Sumario: | The structure of phycobiliproteins and their spatial organization in the phycobilisome provide the environment for high efficiency in light harvesting and conduction towards photosystem II. This article focuses on the analysis of R-phycoerythrin, a light harvesting hexameric phycobiliprotein that is part of the phycobilisomes. The interaction surfaces and the environment of the chromophores of R-phycoerythrin were studied in order to explain its structural stability and spectroscopic sensitivity, properties revealed by perturbation experiments. Three interaction surfaces are described (ab), (ab)3 and (ab)6. The analysis shows the importance of a subunits in the interaction between trimers, the homodimeric nature of the monomer (ab) and also the presence of anchor points in every interaction surface studied: a18Phe and b18Tyr for (ab), b76Asn for (ab)3 and a25Asn for (ab)6 . Side chains of arginine, lysine or glutamine residues are located in the proximity of the chromophores providing the correct stabilization of their carboxylates. Aspartic acids residues are associated through H-bonds to the N atom of the two central rings of the tetrapyrrolic chromophores. Changes in the spectroscopic properties are observed in perturbation experiments, confirming the spatial requirement for an efficient resonance energy transfer among chromophores and through the phycobilisome |
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