6Y3D
X-ray structure of thermophilic C-phycocyanin from Galdiera phlegrea
This is a non-PDB format compatible entry.
Summary for 6Y3D
| Entry DOI | 10.2210/pdb6y3d/pdb |
| Descriptor | C-phycocyanin alpha chain, C-phycocyanin beta chain, PHYCOCYANOBILIN, ... (6 entities in total) |
| Functional Keywords | red algae, c-phycocyanin, pigment, fluorescent, phycobilisomes, fluorescent protein |
| Biological source | Cyanidium caldarium More |
| Total number of polymer chains | 12 |
| Total formula weight | 223590.69 |
| Authors | Ferraro, G.,Lucignano, R.,Marseglia, A.,Merlino, A. (deposition date: 2020-02-18, release date: 2020-12-30, Last modification date: 2024-01-24) |
| Primary citation | Ferraro, G.,Imbimbo, P.,Marseglia, A.,Lucignano, R.,Monti, D.M.,Merlino, A. X-ray structure of C-phycocyanin from Galdieria phlegrea: Determinants of thermostability and comparison with a C-phycocyanin in the entire phycobilisome. Biochim Biophys Acta Bioenerg, 1861:148236-148236, 2020 Cited by PubMed Abstract: Galdieria phlegrea is a polyextremophilic red alga belonging to Cyanidiophyceae. Galdieria phlegrea C-phycocyanin (GpPC), an abundant light-harvesting pigment with an important role in energy capture and transfer to photosystems, is the C-phycocyanin (C-PC) with the highest thermal stability described so far. GpPC also presents interesting antioxidant and anticancer activities. The X-ray structure of the protein was here solved. GpPC is a [(αβ)] hexamer, with the phycocyanobilin chromophore attached to Cys84α, Cys82β and Cys153β. Details of geometry and interaction with solvent of the chromophores are reported. Comparison with the structure of a C-PC in the entire Porphyridium purpureum phycobilisome system reveals that linker polypeptides have a significant effect on the local structure of the chromophores environment. Comparative analyses with the structures of other purified C-PCs, which were carried out including re-refined models of G. sulphuraria C-PC, reveal that GpPC presents a significantly higher number of inter-trimer salt bridges. Notably, the higher number of salt bridges at the (αβ)/(αβ) interface is not due to an increased number of charged residues in this region, but to subtle conformational variations of their side chains, which are the result of mutations of close polar and non-polar residues. PubMed: 32479753DOI: 10.1016/j.bbabio.2020.148236 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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