7D6W
Crystal structure of Phycocyanin from Synechococcus sp. R42DM
7D6W の概要
| エントリーDOI | 10.2210/pdb7d6w/pdb |
| 分子名称 | Phycocyanin alpha subunit, Phycocyanin beta subunit, PHYCOCYANOBILIN, ... (4 entities in total) |
| 機能のキーワード | light harvesting property, photosynthesis |
| 由来する生物種 | Synechococcus sp. R42DM 詳細 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 222652.01 |
| 構造登録者 | Patel, S.N.,Sonani, R.R.,Chaubey, M.G.,Singh, N.K.,Kumar, V.,Madamwar, D. (登録日: 2020-10-02, 公開日: 2021-10-06, 最終更新日: 2023-11-29) |
| 主引用文献 | Patel, 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: 37366498DOI: 10.1007/s13205-023-03665-1 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.15 Å) |
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