9EYS
Structure of Far-Red Photosystem I from C. thermalis PCC 7203
Summary for 9EYS
| Entry DOI | 10.2210/pdb9eys/pdb |
| EMDB information | 50063 |
| Descriptor | Photosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XI, Photosystem I reaction center subunit XII, ... (24 entities in total) |
| Functional Keywords | chlorophyll f, photosystem i, far-red, cyanobacteria, photosynthesis |
| Biological source | Chroococcidiopsis thermalis PCC 7203 More |
| Total number of polymer chains | 36 |
| Total formula weight | 1111568.36 |
| Authors | Consoli, G.,Tufaill, F.,Murray, J.W.,Fantuzzi, A.,Rutherford, A.W. (deposition date: 2024-04-09, release date: 2025-04-23, Last modification date: 2025-12-24) |
| Primary citation | Consoli, G.,Tufail, F.,Leong, H.F.,Viola, S.,Davis, G.A.,Rew, N.,Medranda, D.,Hofer, M.,Simpson, P.,Sandrin, M.,Chachuat, B.,Nelson, J.,Renger, T.,Murray, J.W.,Fantuzzi, A.,Rutherford, A.W. Locating the missing chlorophylls f in far-red photosystem I. Science, 390:eado6830-eado6830, 2025 Cited by PubMed Abstract: The discovery of chlorophyll f-containing photosystems, with their long-wavelength photochemistry, represented a distinct, low-energy paradigm for oxygenic photosynthesis. Structural studies on chlorophyll f-containing photosystem I could identify some chlorophylls f sites, but none among the photochemically active pigments and concluded that chlorophyll f plays no photochemical role. Here, we report two cryo-EM structures of far-red PSI from PCC 7203, allowing the assignment of eight chlorophylls f molecules, including the redox active A. Simulations of absorption difference spectra induced by charge separation indicate that the experimental spectra can be reproduced only by considering the presence of a chlorophyll f at the A site. The chlorophyll f locations, wavelength assignments, and conserved far-red-specific residues provide functional insights for efficient use of long wavelength photons. PubMed: 41066538DOI: 10.1126/science.ado6830 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.01 Å) |
Structure validation
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