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7VEA

Pentacylindrical allophycocyanin core from Thermosynechococcus vulcanus

This is a non-PDB format compatible entry.
Summary for 7VEA
Entry DOI10.2210/pdb7vea/pdb
EMDB information31944
DescriptorAllophycocyanin alpha chain, Allophycocyanin beta chain, Phycobiliprotein ApcE, ... (6 entities in total)
Functional Keywordslight-harvesting complex, phycobilisome, energy transfer, photosynthesis
Biological sourceThermosynechococcus vestitus BP-1
More
Total number of polymer chains90
Total formula weight1787560.23
Authors
Kawakami, K.,Hamaguchi, T.,Hirose, Y.,Kosumi, D.,Miyata, M.,Kamiya, N.,Yonekura, K. (deposition date: 2021-09-08, release date: 2022-06-22, Last modification date: 2022-08-17)
Primary citationKawakami, K.,Hamaguchi, T.,Hirose, Y.,Kosumi, D.,Miyata, M.,Kamiya, N.,Yonekura, K.
Core and rod structures of a thermophilic cyanobacterial light-harvesting phycobilisome.
Nat Commun, 13:3389-3389, 2022
Cited by
PubMed Abstract: Cyanobacteria, glaucophytes, and rhodophytes utilize giant, light-harvesting phycobilisomes (PBSs) for capturing solar energy and conveying it to photosynthetic reaction centers. PBSs are compositionally and structurally diverse, and exceedingly complex, all of which pose a challenge for a comprehensive understanding of their function. To date, three detailed architectures of PBSs by cryo-electron microscopy (cryo-EM) have been described: a hemiellipsoidal type, a block-type from rhodophytes, and a cyanobacterial hemidiscoidal-type. Here, we report cryo-EM structures of a pentacylindrical allophycocyanin core and phycocyanin-containing rod of a thermophilic cyanobacterial hemidiscoidal PBS. The structures define the spatial arrangement of protein subunits and chromophores, crucial for deciphering the energy transfer mechanism. They reveal how the pentacylindrical core is formed, identify key interactions between linker proteins and the bilin chromophores, and indicate pathways for unidirectional energy transfer.
PubMed: 35715389
DOI: 10.1038/s41467-022-30962-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.7 Å)
Structure validation

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