8DDY
Helical rods of far-red light-absorbing allophycocyanin in Synechococcus sp.
8DDY の概要
| エントリーDOI | 10.2210/pdb8ddy/pdb |
| EMDBエントリー | 27382 |
| 分子名称 | Allophycocyanin subunit alpha, Allophycocyanin subunit beta, PHYCOCYANOBILIN, ... (5 entities in total) |
| 機能のキーワード | allophycocyanin, phycobiliprotein, photosystem, photosynthesis, energy transfer, cyanobacteria, far-red light, farlip, lolip |
| 由来する生物種 | Synechococcus sp. 63AY4M1 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 118354.99 |
| 構造登録者 | Gisriel, C.J.,Shen, G.S.,Soulier, N.T.,Flesher, D.A.,Brudvig, G.W.,Bryant, D.A. (登録日: 2022-06-19, 公開日: 2023-04-05) |
| 主引用文献 | Gisriel, C.J.,Elias, E.,Shen, G.,Soulier, N.T.,Flesher, D.A.,Gunner, M.R.,Brudvig, G.W.,Croce, R.,Bryant, D.A. Helical allophycocyanin nanotubes absorb far-red light in a thermophilic cyanobacterium. Sci Adv, 9:eadg0251-eadg0251, 2023 Cited by PubMed Abstract: To compete in certain low-light environments, some cyanobacteria express a paralog of the light-harvesting phycobiliprotein, allophycocyanin (AP), that strongly absorbs far-red light (FRL). Using cryo-electron microscopy and time-resolved absorption spectroscopy, we reveal the structure-function relationship of this FRL-absorbing AP complex (FRL-AP) that is expressed during acclimation to low light and that likely associates with chlorophyll a-containing photosystem I. FRL-AP assembles as helical nanotubes rather than typical toroids due to alterations of the domain geometry within each subunit. Spectroscopic characterization suggests that FRL-AP nanotubes are somewhat inefficient antenna; however, the enhanced ability to harvest FRL when visible light is severely attenuated represents a beneficial trade-off. The results expand the known diversity of light-harvesting proteins in nature and exemplify how biological plasticity is achieved by balancing resource accessibility with efficiency. PubMed: 36961897DOI: 10.1126/sciadv.adg0251 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.89 Å) |
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