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-Structure paper
タイトル | Helical allophycocyanin nanotubes absorb far-red light in a thermophilic cyanobacterium. |
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ジャーナル・号・ページ | Sci Adv, Vol. 9, Issue 12, Page eadg0251, Year 2023 |
掲載日 | 2023年3月24日 |
著者 | Christopher J Gisriel / Eduard Elias / Gaozhong Shen / Nathan T Soulier / David A Flesher / M R Gunner / Gary W Brudvig / Roberta Croce / Donald A Bryant / |
PubMed 要旨 | 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 ...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. |
リンク | Sci Adv / PubMed:36961897 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.89 Å |
構造データ | EMDB-27382, PDB-8ddy: |
化合物 | ChemComp-CYC: ChemComp-CL: ChemComp-HOH: |
由来 |
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キーワード | PHOTOSYNTHESIS / Allophycocyanin / phycobiliprotein / photosystem / energy transfer / cyanobacteria / far-red light / FaRLiP / LoLiP |