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6JO6

Structure of the green algal photosystem I supercomplex with light-harvesting complex I

Summary for 6JO6
Entry DOI10.2210/pdb6jo6/pdb
EMDB information9854
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit psaK, chloroplastic, Photosystem I reaction center subunit XI, ... (28 entities in total)
Functional Keywordsphotosystem membrane protein, photosynthesis
Biological sourceChlamydomonas reinhardtii (Chlamydomonas smithii)
More
Total number of polymer chains19
Total formula weight696899.02
Authors
Suga, M.,Miyazaki, N.,Takahashi, Y. (deposition date: 2019-03-20, release date: 2019-06-19, Last modification date: 2025-06-25)
Primary citationSuga, M.,Ozawa, S.I.,Yoshida-Motomura, K.,Akita, F.,Miyazaki, N.,Takahashi, Y.
Structure of the green algal photosystem I supercomplex with a decameric light-harvesting complex I.
Nat.Plants, 5:626-636, 2019
Cited by
PubMed Abstract: In plants and green algae, the core of photosystem I (PSI) is surrounded by a peripheral antenna system consisting of light-harvesting complex I (LHCI). Here we report the cryo-electron microscopic structure of the PSI-LHCI supercomplex from the green alga Chlamydomonas reinhardtii. The structure reveals that eight Lhca proteins form two tetrameric LHCI belts attached to the PsaF side while the other two Lhca proteins form an additional Lhca2/Lhca9 heterodimer attached to the opposite side. The spatial arrangement of light-harvesting pigments reveals that Chlorophylls b are more abundant in the outer LHCI belt than in the inner LHCI belt and are absent from the core, thereby providing the downhill energy transfer pathways to the PSI core. PSI-LHCI is complexed with a plastocyanin on the patch of lysine residues of PsaF at the luminal side. The assembly provides a structural basis for understanding the mechanism of light-harvesting, excitation energy transfer of the PSI-LHCI supercomplex and electron transfer with plastocyanin.
PubMed: 31182847
DOI: 10.1038/s41477-019-0438-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

240971

數據於2025-08-27公開中

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