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8WQL

In situ PBS-PSII supercomplex from cyanobacterial Spirulina platensis

This is a non-PDB format compatible entry.
Summary for 8WQL
Entry DOI10.2210/pdb8wql/pdb
EMDB information37749
DescriptorLRC1, Cytochrome b559 subunit alpha, Cytochrome b559 subunit beta, ... (48 entities in total)
Functional Keywordscomplex, photosynthesis
Biological sourceArthrospira sp. FACHB-439
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Total number of polymer chains445
Total formula weight8522496.38
Authors
You, X.,Zhang, X.,Xiao, Y.N.,Sun, S.,Sui, S.F. (deposition date: 2023-10-11, release date: 2024-07-31, Last modification date: 2025-09-17)
Primary citationZhang, X.,Xiao, Y.,You, X.,Sun, S.,Sui, S.F.
In situ structural determination of cyanobacterial phycobilisome-PSII supercomplex by STAgSPA strategy.
Nat Commun, 15:7201-7201, 2024
Cited by
PubMed Abstract: Photosynthesis converting solar energy to chemical energy is one of the most important chemical reactions on earth. In cyanobacteria, light energy is captured by antenna system phycobilisomes (PBSs) and transferred to photosynthetic reaction centers of photosystem II (PSII) and photosystem I (PSI). While most of the protein complexes involved in photosynthesis have been characterized by in vitro structural analyses, how these protein complexes function together in vivo is not well understood. Here we implemented STAgSPA, an in situ structural analysis strategy, to solve the native structure of PBS-PSII supercomplex from the cyanobacteria Arthrospira sp. FACHB439 at resolution of ~3.5 Å. The structure reveals coupling details among adjacent PBSs and PSII dimers, and the collaborative energy transfer mechanism mediated by multiple super-PBS in cyanobacteria. Our results provide insights into the diversity of photosynthesis-related systems between prokaryotic cyanobacteria and eukaryotic red algae but are also a methodological demonstration for high-resolution structural analysis in cellular or tissue samples.
PubMed: 39169020
DOI: 10.1038/s41467-024-51460-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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