Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM

Isolated phycobilisome (PBS) sub-assemblies have been widely subjected to X-ray crystallography analysis to obtain greater insights into the structure-function relationship of this light harvesting complex. Allophycocyanin (APC) is the phycobiliprotein always found in the PBS core complex. Phycocyan...

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Publicado no:PLoS One
Main Authors: Sonani, Ravi Raghav, Gupta, Gagan Deep, Madamwar, Datta, Kumar, Vinay
Formato: Artigo
Idioma:Inglês
Publicado em: Public Library of Science 2015
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Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC4414346/
https://ncbi.nlm.nih.gov/pubmed/25923120
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0124580
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spelling pubmed-44143462015-05-07 Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM Sonani, Ravi Raghav Gupta, Gagan Deep Madamwar, Datta Kumar, Vinay PLoS One Research Article Isolated phycobilisome (PBS) sub-assemblies have been widely subjected to X-ray crystallography analysis to obtain greater insights into the structure-function relationship of this light harvesting complex. Allophycocyanin (APC) is the phycobiliprotein always found in the PBS core complex. Phycocyanobilin (PCB) chromophores, covalently bound to conserved Cys residues of α- and β- subunits of APC, are responsible for solar energy absorption from phycocyanin and for transfer to photosynthetic apparatus. In the known APC structures, heterodimers of α- and β- subunits (known as αβ monomers) assemble as trimer or hexamer. We here for the first time report the crystal structure of APC isolated from a marine cyanobacterium (Phormidium sp. A09DM). The crystal structure has been refined against all the observed data to the resolution of 2.51 Å to R(work) (R(free)) of 0.158 (0.229) with good stereochemistry of the atomic model. The Phormidium protein exists as a trimer of αβ monomers in solution and in crystal lattice. The overall tertiary structures of α- and β- subunits, and trimeric quaternary fold of the Phormidium protein resemble the other known APC structures. Also, configuration and conformation of the two covalently bound PCB chromophores in the marine APC are same as those observed in fresh water cyanobacteria and marine red algae. More hydrophobic residues, however, constitute the environment of the chromophore bound to α-subunit of the Phormidium protein, owing mainly to amino acid substitutions in the marine protein. Public Library of Science 2015-04-29 /pmc/articles/PMC4414346/ /pubmed/25923120 http://dx.doi.org/10.1371/journal.pone.0124580 Text en © 2015 Sonani et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
institution US NLM
collection PubMed Central
language Inglês
format Artigo
topic Research Article
spellingShingle Research Article
Sonani, Ravi Raghav
Gupta, Gagan Deep
Madamwar, Datta
Kumar, Vinay
Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM
description Isolated phycobilisome (PBS) sub-assemblies have been widely subjected to X-ray crystallography analysis to obtain greater insights into the structure-function relationship of this light harvesting complex. Allophycocyanin (APC) is the phycobiliprotein always found in the PBS core complex. Phycocyanobilin (PCB) chromophores, covalently bound to conserved Cys residues of α- and β- subunits of APC, are responsible for solar energy absorption from phycocyanin and for transfer to photosynthetic apparatus. In the known APC structures, heterodimers of α- and β- subunits (known as αβ monomers) assemble as trimer or hexamer. We here for the first time report the crystal structure of APC isolated from a marine cyanobacterium (Phormidium sp. A09DM). The crystal structure has been refined against all the observed data to the resolution of 2.51 Å to R(work) (R(free)) of 0.158 (0.229) with good stereochemistry of the atomic model. The Phormidium protein exists as a trimer of αβ monomers in solution and in crystal lattice. The overall tertiary structures of α- and β- subunits, and trimeric quaternary fold of the Phormidium protein resemble the other known APC structures. Also, configuration and conformation of the two covalently bound PCB chromophores in the marine APC are same as those observed in fresh water cyanobacteria and marine red algae. More hydrophobic residues, however, constitute the environment of the chromophore bound to α-subunit of the Phormidium protein, owing mainly to amino acid substitutions in the marine protein.
author Sonani, Ravi Raghav
Gupta, Gagan Deep
Madamwar, Datta
Kumar, Vinay
author_facet Sonani, Ravi Raghav
Gupta, Gagan Deep
Madamwar, Datta
Kumar, Vinay
author_sort Sonani, Ravi Raghav
title Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM
title_short Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM
title_full Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM
title_fullStr Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM
title_full_unstemmed Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM
title_sort crystal structure of allophycocyanin from marine cyanobacterium phormidium sp. a09dm
publisher Public Library of Science
container_title PLoS One
publishDate 2015
url https://ncbi.nlm.nih.gov/pmc/articles/PMC4414346/
https://ncbi.nlm.nih.gov/pubmed/25923120
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0124580
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