7EYD

Cryo-EM structure of cyanobacterial phycobilisome from Anabaena sp. PCC 7120

これはPDB形式変換不可エントリーです。

7EYD の概要

• エントリーDOI: 10.2210/pdb7eyd/pdb
• EMDBエントリー: 31373 31381
• 分子名称: Phycobilisome rod-core linker polypeptide CpcG2, Phycobiliprotein ApcE, Allophycocyanin subunit beta-18, ... (13 entities in total)
• 機能のキーワード: photosynthesis
• 由来する生物種: Nostoc sp. PCC 7120 = FACHB-418; 詳細
• タンパク質・核酸の鎖数: 288
• 化学式量合計: 5666114.10

構造登録者

Zheng, L.,Zheng, Z.,Li, X.,Wang, G.,Zhang, K.,Wei, P.,Zhao, J.,Gao, N. (登録日: 2021-05-30, 公開日: 2021-10-06, 最終更新日: 2025-09-17)

主引用文献

Zheng, L.,Zheng, Z.,Li, X.,Wang, G.,Zhang, K.,Wei, P.,Zhao, J.,Gao, N.
Structural insight into the mechanism of energy transfer in cyanobacterial phycobilisomes.
Nat Commun, 12:5497-5497, 2021

PubMed Abstract: Phycobilisomes (PBS) are the major light-harvesting machineries for photosynthesis in cyanobacteria and red algae and they have a hierarchical structure of a core and peripheral rods, with both consisting of phycobiliproteins and linker proteins. Here we report the cryo-EM structures of PBS from two cyanobacterial species, Anabaena 7120 and Synechococcus 7002. Both PBS are hemidiscoidal in shape and share a common triangular core structure. While the Anabaena PBS has two additional hexamers in the core linked by the 4th linker domain of ApcE (L). The PBS structures predict that, compared with the PBS from red algae, the cyanobacterial PBS could have more direct routes for energy transfer to ApcD. Structure-based systematic mutagenesis analysis of the chromophore environment of ApcD and ApcF subunits reveals that aromatic residues are critical to excitation energy transfer (EET). The structures also suggest that the linker protein could actively participate in the process of EET in both rods and the cores. These results provide insights into the organization of chromophores and the mechanisms of EET within cyanobacterial PBS.

PubMed: 34535665
DOI: 10.1038/s41467-021-25813-y

実験手法

ELECTRON MICROSCOPY (3.9 Å)