9LUT

PSI-LHCI supercomplex binding with 4 Lhcas from M. polymorpha

Summary for 9LUT

• Entry DOI: 10.2210/pdb9lut/pdb
• EMDB information: 63404
• Descriptor: Chlorophyll a-b binding protein, chloroplastic, Photosystem I reaction center subunit III, Photosystem I reaction center subunit V, chloroplastic, ... (30 entities in total)
• Functional Keywords: photosystem i, light-harvasting complex, photosynthesis
• Biological source: Marchantia polymorpha (liverwort); More
• Total number of polymer chains: 17
• Total formula weight: 597376.06

Authors

Tsai, P.-C.,La Rocca, R.,Shen, J.-R.,Akita, F. (deposition date: 2025-02-10, release date: 2026-02-18)

Primary citation

Tsai, P.C.,La Rocca, R.,Motose, H.,Shen, J.R.,Akita, F.
Structural study of monomeric and dimeric photosystem I-LHCI supercomplexes from a bryophyte.
Commun Biol, 9:146-146, 2026

PubMed Abstract: Photosystem I (PSI) is one of the two photosystems conserved from cyanobacteria to vascular plants, and associates with multiple light-harvesting complexes (LHCs) that capture and transfer solar energy. Liverworts such as Marchantia polymorpha occupy an early evolutionary position among land plants and faced major challenges during terrestrial adaptation, including desiccation, strong light, and UV radiation. We reveal the cryo-electron microscopic structures of PSI-LHCI monomer and homodimer from the liverwort M. polymorpha at resolutions of 1.94 and 2.52 Å, respectively. The high-resolution map allows identification of the cofactors of the monomer and reveal differences between the liverwort and moss, another clade of bryophytes. The PSI-LHCI monomer-monomer is stabilized by PsaG and PsaH interactions on the stromal side, which causes the bending and twisting of the homodimer. PsaM interacts with PsaB tightly, indicating a key role of PsaM in mediating the dimerization.

PubMed: 41644713
DOI: 10.1038/s42003-026-09631-w

Experimental method

ELECTRON MICROSCOPY (1.94 Å)