9SE6
Structure of Photosystem I from Chlamydomonas reinhardtii at 1.83 A resolution
Summary for 9SE6
| Entry DOI | 10.2210/pdb9se6/pdb |
| Related | 9se7 |
| EMDB information | 54803 |
| Descriptor | Light-harvesting chlorophyll-a/b protein of photosystem I, type III, Photosystem I reaction center subunit II, chloroplastic, Photosystem I reaction center subunit IV, chloroplastic, ... (32 entities in total) |
| Functional Keywords | photosystem i, chlamydomonas reinhardtii, cryoem, photosynthesis |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 19 |
| Total formula weight | 697983.49 |
| Authors | Mahapatra, G.P.,Schuller, J.M. (deposition date: 2025-08-15, release date: 2026-04-01, Last modification date: 2026-04-08) |
| Primary citation | Ogawa, Y.,Mahapatra, G.P.,Milrad, Y.,Schimpf, M.,Kurisu, G.,Hippler, M.,Schuller, J.M. Cryo-EM structure of Chlamydomonas reinhardtii Photosystem I complexed with cytochrome c 6 . Nat Commun, 2026 Cited by PubMed Abstract: Photosynthetic electron transfer relies on small soluble carriers that shuttle electrons between the cytochrome b₆f complex and Photosystem I (PSI). While copper-containing plastocyanin (Pc) serves this role in plants, the heme protein cytochrome c₆ (Cyt c₆) is also employed in algae and cyanobacteria. Here, we present a cryo-electron microscopy structure of a Cyt c₆:PSI complex from Chlamydomonas reinhardtii. We observe that the heme group of Cyt c₆ is positioned ~11 Å away from P700, stabilized by extensive contacts involving a N-terminal helix-loop-helix motif of PSAF, characteristic of eukaryotic PSI. Notably, the algal Cyt c₆ also retains an arginine residue (R66) which is crucial for cyanobacterial donor:PSI reactions. Our structure reveals the previously uncharacterized interactions involving this residue; it can form a putative electrostatic contact with PsaB-D623 while also contributing to a tri-planar π(cation)-π interactions with adjacent residues. Our findings provide a structural framework for understanding the mechanism and evolution of donor:PSI interactions. PubMed: 41896549DOI: 10.1038/s41467-026-70944-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.83 Å) |
Structure validation
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