Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9SE6

Structure of Photosystem I from Chlamydomonas reinhardtii at 1.83 A resolution

Summary for 9SE6
Entry DOI10.2210/pdb9se6/pdb
Related9se7
EMDB information54803
DescriptorLight-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 Keywordsphotosystem i, chlamydomonas reinhardtii, cryoem, photosynthesis
Biological sourceChlamydomonas reinhardtii
More
Total number of polymer chains19
Total formula weight697983.49
Authors
Mahapatra, G.P.,Schuller, J.M. (deposition date: 2025-08-15, release date: 2026-04-01, Last modification date: 2026-04-08)
Primary citationOgawa, 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: 41896549
DOI: 10.1038/s41467-026-70944-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (1.83 Å)
Structure validation

251801

건을2026-04-08부터공개중

PDB statisticsPDBj update infoContact PDBjnumon