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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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2015-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0124580 |
| _version_ | 1818727329640218624 |
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| author | Ravi Raghav Sonani Gagan Deep Gupta Datta Madamwar Vinay Kumar |
| author_facet | Ravi Raghav Sonani Gagan Deep Gupta Datta Madamwar Vinay Kumar |
| author_sort | Ravi Raghav Sonani |
| collection | DOAJ |
| 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 Rwork (Rfree) 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. |
| first_indexed | 2024-12-17T22:12:22Z |
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| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-17T22:12:22Z |
| publishDate | 2015-01-01 |
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| spelling | doaj.art-41628700de24405486c0b528f0771ac92022-12-21T21:30:42ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01104e012458010.1371/journal.pone.0124580Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM.Ravi Raghav SonaniGagan Deep GuptaDatta MadamwarVinay KumarIsolated 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 Rwork (Rfree) 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.https://doi.org/10.1371/journal.pone.0124580 |
| spellingShingle | Ravi Raghav Sonani Gagan Deep Gupta Datta Madamwar Vinay Kumar Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM. PLoS ONE |
| title | 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_short | Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM. |
| title_sort | crystal structure of allophycocyanin from marine cyanobacterium phormidium sp a09dm |
| url | https://doi.org/10.1371/journal.pone.0124580 |
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