6KGX の概要
| エントリーDOI | 10.2210/pdb6kgx/pdb |
| EMDBエントリー | 34529 9976 9977 9978 9979 9980 9981 9982 9983 9984 9985 9986 9987 9988 |
| 分子名称 | Phycoerythrin alpha subunit, C-phycocyanin beta subunit, LR2, ... (28 entities in total) |
| 機能のキーワード | phycobilisome, complex, photosynthesis |
| 由来する生物種 | Porphyridium purpureum (Red alga) 詳細 |
| タンパク質・核酸の鎖数 | 706 |
| 化学式量合計 | 14789615.74 |
| 構造登録者 | |
| 主引用文献 | Ma, J.F.,You, X.,Sun, S.,Wang, X.X.,Qin, S.,Sui, S.F. Structural basis of energy transfer in Porphyridium purpureum phycobilisome. Nature, 579:146-151, 2020 Cited by PubMed Abstract: Photosynthetic organisms have developed various light-harvesting systems to adapt to their environments. Phycobilisomes are large light-harvesting protein complexes found in cyanobacteria and red algae, although how the energies of the chromophores within these complexes are modulated by their environment is unclear. Here we report the cryo-electron microscopy structure of a 14.7-megadalton phycobilisome with a hemiellipsoidal shape from the red alga Porphyridium purpureum. Within this complex we determine the structures of 706 protein subunits, including 528 phycoerythrin, 72 phycocyanin, 46 allophycocyanin and 60 linker proteins. In addition, 1,598 chromophores are resolved comprising 1,430 phycoerythrobilin, 48 phycourobilin and 120 phycocyanobilin molecules. The markedly improved resolution of our structure compared with that of the phycobilisome of Griffithsia pacifica enabled us to build an accurate atomic model of the P. purpureum phycobilisome system. The model reveals how the linker proteins affect the microenvironment of the chromophores, and suggests that interactions of the aromatic amino acids of the linker proteins with the chromophores may be a key factor in fine-tuning the energy states of the chromophores to ensure the efficient unidirectional transfer of energy. PubMed: 32076272DOI: 10.1038/s41586-020-2020-7 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.8 Å) |
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