7DR0
Structure of Wild-type PSI monomer1 from Cyanophora paradoxa
Summary for 7DR0
| Entry DOI | 10.2210/pdb7dr0/pdb |
| EMDB information | 30820 |
| Descriptor | Photosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XI, Photosystem I reaction center subunit XII, ... (18 entities in total) |
| Functional Keywords | photosystem i, electron transport, photosynthesis |
| Biological source | Cyanophora paradoxa More |
| Total number of polymer chains | 11 |
| Total formula weight | 359127.01 |
| Authors | Kato, K.,Nagao, R.,Akita, F.,Miyazaki, N.,Shen, J.R. (deposition date: 2020-12-25, release date: 2022-02-16, Last modification date: 2025-11-19) |
| Primary citation | Kato, K.,Nagao, R.,Ueno, Y.,Yokono, M.,Suzuki, T.,Jiang, T.Y.,Dohmae, N.,Akita, F.,Akimoto, S.,Miyazaki, N.,Shen, J.R. Structure of a tetrameric photosystem I from a glaucophyte alga Cyanophora paradoxa. Nat Commun, 13:1679-1679, 2022 Cited by PubMed Abstract: Photosystem I (PSI) is one of the two photosystems functioning in light-energy harvesting, transfer, and electron transfer in photosynthesis. However, the oligomerization state of PSI is variable among photosynthetic organisms. We present a 3.8-Å resolution cryo-electron microscopic structure of tetrameric PSI isolated from the glaucophyte alga Cyanophora paradoxa, which reveals differences with PSI from other organisms in subunit composition and organization. The PSI tetramer is organized in a dimer of dimers with a C2 symmetry. Unlike cyanobacterial PSI tetramers, two of the four monomers are rotated around 90°, resulting in a completely different pattern of monomer-monomer interactions. Excitation-energy transfer among chlorophylls differs significantly between Cyanophora and cyanobacterial PSI tetramers. These structural and spectroscopic features reveal characteristic interactions and excitation-energy transfer in the Cyanophora PSI tetramer, suggesting that the Cyanophora PSI could represent a turning point in the evolution of PSI from prokaryotes to eukaryotes. PubMed: 35354806DOI: 10.1038/s41467-022-29303-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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