8XR6
Cryo-EM structure of cryptophyte photosystem II
Summary for 8XR6
Entry DOI | 10.2210/pdb8xr6/pdb |
EMDB information | 38596 |
Descriptor | Photosystem II protein D1, Photosystem II D2 protein, Cytochrome b559 subunit alpha, ... (45 entities in total) |
Functional Keywords | cryptophyte, photosystem ii, evolution, photosynthesis |
Biological source | Chroomonas placoidea More |
Total number of polymer chains | 56 |
Total formula weight | 1325072.89 |
Authors | Li, K.,Zhao, L.S.,Zhang, Y.Z.,Liu, L.N. (deposition date: 2024-01-06, release date: 2024-06-19, Last modification date: 2025-01-01) |
Primary citation | Zhang, Y.Z.,Li, K.,Qin, B.Y.,Guo, J.P.,Zhang, Q.B.,Zhao, D.L.,Chen, X.L.,Gao, J.,Liu, L.N.,Zhao, L.S. Structure of cryptophyte photosystem II-light-harvesting antennae supercomplex. Nat Commun, 15:4999-4999, 2024 Cited by PubMed Abstract: Cryptophytes are ancestral photosynthetic organisms evolved from red algae through secondary endosymbiosis. They have developed alloxanthin-chlorophyll a/c2-binding proteins (ACPs) as light-harvesting complexes (LHCs). The distinctive properties of cryptophytes contribute to efficient oxygenic photosynthesis and underscore the evolutionary relationships of red-lineage plastids. Here we present the cryo-electron microscopy structure of the Photosystem II (PSII)-ACPII supercomplex from the cryptophyte Chroomonas placoidea. The structure includes a PSII dimer and twelve ACPII monomers forming four linear trimers. These trimers structurally resemble red algae LHCs and cryptophyte ACPI trimers that associate with Photosystem I (PSI), suggesting their close evolutionary links. We also determine a Chl a-binding subunit, Psb-γ, essential for stabilizing PSII-ACPII association. Furthermore, computational calculation provides insights into the excitation energy transfer pathways. Our study lays a solid structural foundation for understanding the light-energy capture and transfer in cryptophyte PSII-ACPII, evolutionary variations in PSII-LHCII, and the origin of red-lineage LHCIIs. PubMed: 38866834DOI: 10.1038/s41467-024-49453-0 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.53 Å) |
Structure validation
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