9T5T
Chlorophyll f-containing dimeric far-red Photosystem II from Chroococcidiopsis thermalis PCC 7203
Summary for 9T5T
| Entry DOI | 10.2210/pdb9t5t/pdb |
| Related | 9T5U |
| EMDB information | 55593 |
| Descriptor | Photosystem II protein D1, Photosystem II reaction center protein J, Photosystem II reaction center protein K, ... (39 entities in total) |
| Functional Keywords | chlorophyll f, photosystem ii, electron transport, farlip |
| Biological source | Chroococcidiopsis thermalis PCC 7203 More |
| Total number of polymer chains | 42 |
| Total formula weight | 792560.72 |
| Authors | Leong, H.F.,Consoli, G.,Murray, J.W.,Fantuzzi, A.,Rutherford, A.W. (deposition date: 2025-11-05, release date: 2026-06-10, Last modification date: 2026-06-17) |
| Primary citation | Leong, H.F.,Consoli, G.,Davis, G.A.,Hancox-Lachman, B.,Renard, K.,Tufail, F.,Lee, L.E.,Gautier, L.,Murray, J.W.,Fantuzzi, A.,Rutherford, A.W. Mapping the absorption landscape of far-red Photosystem II. Nat Commun, 2026 Cited by PubMed Abstract: Far-red light photoacclimation enables some cyanobacteria to survive in white-light-depleted environments by extending the red limit of photosynthesis. In far-red Photosystem II, paralogous subunits replace their canonical counterparts, allowing the incorporation of some chlorophyll f molecules and one chlorophyll d that are red-shifted and spectrally distinct from the chlorophyll a manifold, and from each other. Here, we present a comparative study of far-red Photosystem II from Chroococcidiopsis thermalis PCC 7203 and Calothrix sp. NIES-3974. In C. thermalis, the cryo-electron microscopy structure reveals the far-red-exclusive subunit, PsbH2', which forms part of a chlorophyll f binding site. We also assign four chlorophyll f sites using sequence comparisons and electrostatic potential analyses. In Calothrix, psbH2' is absent, and the same analyses show that only two of these chlorophyll f sites are present. Comparative phylogenetic, structural, and spectroscopic analyses allow the assignment of specific wavelengths to all the red-shifted chlorophylls. This provides the framework needed to model excitation energy transfer in far-red Photosystem II, and to understand the conserved features that allow survival under far-red light. PubMed: 42248907DOI: 10.1038/s41467-026-73964-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.17 Å) |
Structure validation
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