8Z9D

cryo-EM structure of PSII-LHCII megacomplex from spinach

This is a non-PDB format compatible entry.

Summary for 8Z9D

• Entry DOI: 10.2210/pdb8z9d/pdb
• EMDB information: 39860
• Descriptor: Photosystem II protein D1, Photosystem II reaction center protein Z, Chlorophyll a-b binding protein CP24, chloroplastic, ... (46 entities in total)
• Functional Keywords: psii, lhcii, megacomplex, photosynthesis
• Biological source: Spinacia oleracea (spinach); More
• Total number of polymer chains: 112
• Total formula weight: 2986188.26

Authors

Shan, J.Y.,Liu, Z.F. (deposition date: 2024-04-23, release date: 2024-11-13, Last modification date: 2025-02-26)

Primary citation

Shan, J.,Niedzwiedzki, D.M.,Tomar, R.S.,Liu, Z.,Liu, H.
Architecture and functional regulation of a plant PSII-LHCII megacomplex.
Sci Adv, 10:eadq9967-eadq9967, 2024

PubMed Abstract: Photosystem II (PSII) splits water in oxygenic photosynthesis on Earth. The structure and function of the CSM-type PSII-LHCII (light-harvesting complex II) megacomplexes from the wild-type and PsbR-deletion mutant plants are studied through electron microscopy (EM), structural mass spectrometry, and ultrafast fluorescence spectroscopy [time-resolved fluorescence (TRF)]. The cryo-EM structure of a type I CSM megacomplex demonstrates that the three domains of PsbR bind to the stromal side of D1, D2, and CP43; associate with the single transmembrane helix of the redox active Cyt ; and stabilize the luminal extrinsic PsbP, respectively. This megacomplex, with PsbR and PsbY centered around the narrow interface between two dimeric PSII cores, provides the supramolecular structural basis that regulates the plastoquinone occupancy in Q site, excitation energy transfer, and oxygen evolution. PSII-LHCII megacomplexes (types I and II) and LHC aggregation levels in mutant were also interrogated and compared to wild-type plants through EM and picosecond TRF.

PubMed: 39671473
DOI: 10.1126/sciadv.adq9967

Experimental method

ELECTRON MICROSCOPY (3.22 Å)