7F86
Crystal structure of Phycoerythrin from Halomicronema Sp. R31DM
7F86 の概要
| エントリーDOI | 10.2210/pdb7f86/pdb |
| 分子名称 | Phycoerythrin beta subunit, Phycoerythrin alpha subunit, PHYCOERYTHROBILIN, ... (4 entities in total) |
| 機能のキーワード | light harvesting, photosynthesis, phycobiliproteins, cyanobacteria |
| 由来する生物種 | Halomicronema sp. R31DM 詳細 |
| タンパク質・核酸の鎖数 | 24 |
| 化学式量合計 | 480859.33 |
| 構造登録者 | Patel, S.N.,Gupta, G.D.,Sonani, R.R.,Singh, N.K.,Kumar, V.,Madamwar, D. (登録日: 2021-07-01, 公開日: 2022-04-13, 最終更新日: 2025-09-17) |
| 主引用文献 | Patel, S.N.,Sonani, R.R.,Gupta, G.D.,Singh, N.K.,Kumar, V.,Madamwar, D. Crystal structure analysis of phycoerythrin from marine cyanobacterium Halomicronema . J.Biomol.Struct.Dyn., 41:3752-3761, 2023 Cited by PubMed Abstract: Phycoerythrin (PE) is green light-absorbing pigment-protein that assists in efficient light harvesting in cyanobacteria and red-algae. PE in cyanobacteria stays less studied so far as compared to that in red algae. In this study, PE from marine cyanobacteria sp. R31DM is purified and subjected for its structural characterisation by X-ray crystallography in order to understand its light-harvesting characteristics. The crystal structure is solved to a resolution-limit of 2.21 Å with reasonable R-factors values, 0.16/0.21 (R/ R). PE forms hexamer of hetero-dimers made up of two peptide chains, α- and β-subunits containing 2 and 3 phycoerythrobilin (PEB) chromophores covalently attached to them, respectively. Geometry of five chromophores is analysed along with their relative position within the PE hexamer. Also, their interactions with the surrounding microenvironment are analysed. The plausible energy transfer pathways in hexamer structure have been predicted based on relative position and geometry of chromophores. This structure enriches the structural information of cyanobacterial PE in order to understand its light-harvesting capacity.Communicated by Ramaswamy H. Sarma. PubMed: 35354393DOI: 10.1080/07391102.2022.2055647 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.21 Å) |
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