1JBO
The 1.45A Three-Dimensional Structure of c-Phycocyanin from the Thermophylic Cyanobacterium Synechococcus elongatus
1JBO の概要
| エントリーDOI | 10.2210/pdb1jbo/pdb |
| 分子名称 | C-Phycocyanin alpha chain, C-Phycocyanin beta chain, PHYCOCYANOBILIN, ... (4 entities in total) |
| 機能のキーワード | photosynthesis |
| 由来する生物種 | Synechococcus elongatus 詳細 |
| 細胞内の位置 | Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P50032 P50033 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 37439.36 |
| 構造登録者 | Nield, J.,Rizkallah, P.J.,Barber, J.,Chayen, N.E. (登録日: 2002-05-02, 公開日: 2003-03-18, 最終更新日: 2023-08-16) |
| 主引用文献 | Nield, J.,Rizkallah, P.J.,Barber, J.,Chayen, N.E. The 1.45A three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus J.STRUCT.BIOL., 141:149-155, 2003 Cited by PubMed Abstract: The conversion of solar radiation to chemical energy by photosynthetic organisms provides the primary driving force for life on earth. Light energy is captured by a variety of pigments, usually bound to proteins, which vary with different types of organisms. We report here the 1.45 A resolution three-dimensional structure of one such pigment protein, C-phycocyanin, from Synechococcus elongatus. The structure is at the highest resolution achieved for any such phycobiliprotein. This level of resolution was made possible by implementing a novel crystallization method whereby nucleation is decoupled from subsequent growth, by incubating crystallizing drops for 7h under nucleation conditions and then transferring them to metastable conditions for growth. This is done without touching the crystallization drops throughout the process. PubMed: 12615541DOI: 10.1016/S1047-8477(02)00609-3 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.45 Å) |
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