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7YCA

Cryo-EM structure of the PSI-LHCI-Lhcp supercomplex from Ostreococcus tauri

Summary for 7YCA
Entry DOI10.2210/pdb7yca/pdb
EMDB information33737
DescriptorLhca1, Photosystem I reaction center subunit II, chloroplastic, Photosystem I reaction centre subunit IV, ... (39 entities in total)
Functional Keywordscomplex, electron transport, photosynthesis
Biological sourceOstreococcus tauri
More
Total number of polymer chains30
Total formula weight1076390.18
Authors
Shan, J.,Sheng, X.,Ishii, A.,Watanabe, A.,Song, C.,Murata, K.,Minagawa, J.,Liu, Z. (deposition date: 2022-07-01, release date: 2023-04-26, Last modification date: 2024-10-23)
Primary citationIshii, A.,Shan, J.,Sheng, X.,Kim, E.,Watanabe, A.,Yokono, M.,Noda, C.,Song, C.,Murata, K.,Liu, Z.,Minagawa, J.
The photosystem I supercomplex from a primordial green alga Ostreococcus tauri harbors three light-harvesting complex trimers.
Elife, 12:-, 2023
Cited by
PubMed Abstract: As a ubiquitous picophytoplankton in the ocean and an early-branching green alga, is a model prasinophyte species for studying the functional evolution of the light-harvesting systems in photosynthesis. Here, we report the structure and function of the photosystem I (PSI) supercomplex in low light conditions, where it expands its photon-absorbing capacity by assembling with the light-harvesting complexes I (LHCI) and a prasinophyte-specific light-harvesting complex (Lhcp). The architecture of the supercomplex exhibits hybrid features of the plant-type and the green algal-type PSI supercomplexes, consisting of a PSI core, an Lhca1-Lhca4-Lhca2-Lhca3 belt attached on one side and an Lhca5-Lhca6 heterodimer associated on the other side between PsaG and PsaH. Interestingly, nine Lhcp subunits, including one Lhcp1 monomer with a phosphorylated amino-terminal threonine and eight Lhcp2 monomers, oligomerize into three trimers and associate with PSI on the third side between Lhca6 and PsaK. The Lhcp1 phosphorylation and the light-harvesting capacity of PSI were subjected to reversible photoacclimation, suggesting that the formation of PSI-LHCI-Lhcp supercomplex is likely due to a phosphorylation-dependent mechanism induced by changes in light intensity. Notably, this supercomplex did not exhibit far-red peaks in the 77 K fluorescence spectra, which is possibly due to the weak coupling of the chlorophyll 603-609 pair in Lhca1-4.
PubMed: 36951548
DOI: 10.7554/eLife.84488
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.94 Å)
Structure validation

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