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:	MARTÍNEZ-OYANEDEL,JOSÉ, CONTRERAS-MARTEL,CARLOS, BRUNA,CAROLA, BUNSTER,MARTA
Lenguaje:	English
Publicado:	Sociedad de Biología de Chile 2004
Materias:	1eyx anchor points interaction surfaces stability spectroscopic sensitivity
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000500003
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spelling	oai:scielo:S0716-976020040005000032005-06-01Structural-functional analysis of the oligomeric protein R-phycoerythrinMARTÍNEZ-OYANEDEL,JOSÉCONTRERAS-MARTEL,CARLOSBRUNA,CAROLABUNSTER,MARTA 1eyx anchor points interaction surfaces stability spectroscopic sensitivity 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 phycobilisomeinfo:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.37 n.4 suppl.A 20042004-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000500003en10.4067/S0716-97602004000500003
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	1eyx anchor points interaction surfaces stability spectroscopic sensitivity
spellingShingle	1eyx anchor points interaction surfaces stability spectroscopic sensitivity MARTÍNEZ-OYANEDEL,JOSÉ CONTRERAS-MARTEL,CARLOS BRUNA,CAROLA BUNSTER,MARTA Structural-functional analysis of the oligomeric protein R-phycoerythrin
description	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
author	MARTÍNEZ-OYANEDEL,JOSÉ CONTRERAS-MARTEL,CARLOS BRUNA,CAROLA BUNSTER,MARTA
author_facet	MARTÍNEZ-OYANEDEL,JOSÉ CONTRERAS-MARTEL,CARLOS BRUNA,CAROLA BUNSTER,MARTA
author_sort	MARTÍNEZ-OYANEDEL,JOSÉ
title	Structural-functional analysis of the oligomeric protein R-phycoerythrin
title_short	Structural-functional analysis of the oligomeric protein R-phycoerythrin
title_full	Structural-functional analysis of the oligomeric protein R-phycoerythrin
title_fullStr	Structural-functional analysis of the oligomeric protein R-phycoerythrin
title_full_unstemmed	Structural-functional analysis of the oligomeric protein R-phycoerythrin
title_sort	structural-functional analysis of the oligomeric protein r-phycoerythrin
publisher	Sociedad de Biología de Chile
publishDate	2004
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000500003
work_keys_str_mv	AT martinezoyanedeljose structuralfunctionalanalysisoftheoligomericproteinrphycoerythrin AT contrerasmartelcarlos structuralfunctionalanalysisoftheoligomericproteinrphycoerythrin AT brunacarola structuralfunctionalanalysisoftheoligomericproteinrphycoerythrin AT bunstermarta structuralfunctionalanalysisoftheoligomericproteinrphycoerythrin
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Structural-functional analysis of the oligomeric protein R-phycoerythrin

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