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7D6W

Crystal structure of Phycocyanin from Synechococcus sp. R42DM

Summary for 7D6W
Entry DOI10.2210/pdb7d6w/pdb
DescriptorPhycocyanin alpha subunit, Phycocyanin beta subunit, PHYCOCYANOBILIN, ... (4 entities in total)
Functional Keywordslight harvesting property, photosynthesis
Biological sourceSynechococcus sp. R42DM
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Total number of polymer chains12
Total formula weight222652.01
Authors
Patel, S.N.,Sonani, R.R.,Chaubey, M.G.,Singh, N.K.,Kumar, V.,Madamwar, D. (deposition date: 2020-10-02, release date: 2021-10-06, Last modification date: 2023-11-29)
Primary citationPatel, S.N.,Sonani, R.R.,Chaubey, M.G.,Gupta, G.D.,Singh, N.K.,Kumar, V.,Madamwar, D.
Crystal structure of Synechococcus phycocyanin: implications of light-harvesting and antioxidant properties.
3 Biotech, 13:247-247, 2023
Cited by
PubMed Abstract: Phycobiliproteins is a family of chromophore-containing proteins having light-harvesting and antioxidant capacity. The phycocyanin (PC) is a brilliant blue coloured phycobiliprotein, found in rod structure of phycobilisome and has been widely studied for their therapeutic and fluorescent properties. In the present study, the hexameric assembly structure of phycocyanin (Syn-PC) from Sp. R42DM is characterized by X-ray crystallography to understand its light-harvesting and antioxidant properties. The crystal structure of Syn-PC is solved with 2.15 Å resolution and crystallographic -factors, / 0.16/0.21. The hexamer of Syn-PC is formed by heterodimer of two polypeptide chains, namely, α- and β-subunits. The structure is analysed at atomic level to reveal the chromophore microenvironment and possible light energy transfer mechanism in Syn-PC. The chromophore arrangement in hexamer, deviation angle and distance between the chromophore contribute to the energy transfer efficiency of protein. The structural attributes responsible for the antioxidant potential of Syn-PC are recognized and annotated on its 3-dimensional structure.
PubMed: 37366498
DOI: 10.1007/s13205-023-03665-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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数据于2024-12-25公开中

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