8HFQ

Cryo-EM structure of CpcL-PBS from cyanobacterium Synechocystis sp. PCC 6803

8HFQ の概要

• エントリーDOI: 10.2210/pdb8hfq/pdb
• EMDBエントリー: 34724
• 分子名称: C-phycocyanin alpha subunit, C-phycocyanin beta subunit, Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod 1, ... (7 entities in total)
• 機能のキーワード: cpcl-phycobilisome, energy transfer, ferredoxin:nadp+ oxidoreductase, ultrafast spectroscopy, photosynthesis
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa); 詳細
• タンパク質・核酸の鎖数: 40
• 化学式量合計: 813562.60

構造登録者

Zheng, L.,Zhang, Z.,Wang, H.,Zheng, Z.,Gao, N.,Zhao, J. (登録日: 2022-11-11, 公開日: 2023-11-08, 最終更新日: 2025-09-24)

主引用文献

Zheng, L.,Zhang, Z.,Wang, H.,Zheng, Z.,Wang, J.,Liu, H.,Chen, H.,Dong, C.,Wang, G.,Weng, Y.,Gao, N.,Zhao, J.
Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes.
Nat Commun, 14:3961-3961, 2023

PubMed Abstract: Phycobilisomes (PBS) are the major light harvesting complexes of photosynthesis in the cyanobacteria and red algae. CpcL-PBS is a type of small PBS in cyanobacteria that transfers energy directly to photosystem I without the core structure. Here we report the cryo-EM structure of the CpcL-PBS from the cyanobacterium Synechocystis sp. PCC 6803 at 2.6-Å resolution. The structure shows the CpcD domain of ferredoxin: NADP oxidoreductase is located at the distal end of CpcL-PBS, responsible for its attachment to PBS. With the evidence of ultrafast transient absorption and fluorescence spectroscopy, the roles of individual bilins in energy transfer are revealed. The bilin β located near photosystem I has an enhanced planarity and is the red-bilin responsible for the direct energy transfer to photosystem I.

PubMed: 37407580
DOI: 10.1038/s41467-023-39689-7

実験手法

ELECTRON MICROSCOPY (2.64 Å)