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8XR6

Cryo-EM structure of cryptophyte photosystem II

Summary for 8XR6
Entry DOI10.2210/pdb8xr6/pdb
EMDB information38596
DescriptorPhotosystem II protein D1, Photosystem II D2 protein, Cytochrome b559 subunit alpha, ... (45 entities in total)
Functional Keywordscryptophyte, photosystem ii, evolution, photosynthesis
Biological sourceChroomonas placoidea
More
Total number of polymer chains56
Total formula weight1325072.89
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 citationZhang, 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: 38866834
DOI: 10.1038/s41467-024-49453-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.53 Å)
Structure validation

237735

数据于2025-06-18公开中

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