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7Y5E

In situ single-PBS-PSII-PSI-LHCs megacomplex.

This is a non-PDB format compatible entry.
Summary for 7Y5E
Entry DOI10.2210/pdb7y5e/pdb
EMDB information33558 33561 33597 33605 33618
DescriptorPhycoerythrin alpha subunit, C-phycocyanin beta subunit, (2S)-2,3-dihydroxypropyl octadecanoate, ... (104 entities in total)
Functional Keywordscomplex, photosynthesis
Biological sourcePorphyridium purpureum
More
Total number of polymer chains894
Total formula weight18653194.67
Authors
You, X.,Zhang, X.,Cheng, J.,Xiao, Y.N.,Sui, S.F. (deposition date: 2022-06-17, release date: 2023-02-01, Last modification date: 2024-07-03)
Primary citationYou, X.,Zhang, X.,Cheng, J.,Xiao, Y.,Ma, J.,Sun, S.,Zhang, X.,Wang, H.W.,Sui, S.F.
In situ structure of the red algal phycobilisome-PSII-PSI-LHC megacomplex.
Nature, 616:199-206, 2023
Cited by
PubMed Abstract: In oxygenic photosynthetic organisms, light energy is captured by antenna systems and transferred to photosystem II (PSII) and photosystem I (PSI) to drive photosynthesis. The antenna systems of red algae consist of soluble phycobilisomes (PBSs) and transmembrane light-harvesting complexes (LHCs). Excitation energy transfer pathways from PBS to photosystems remain unclear owing to the lack of structural information. Here we present in situ structures of PBS-PSII-PSI-LHC megacomplexes from the red alga Porphyridium purpureum at near-atomic resolution using cryogenic electron tomography and in situ single-particle analysis, providing interaction details between PBS, PSII and PSI. The structures reveal several unidentified and incomplete proteins and their roles in the assembly of the megacomplex, as well as a huge and sophisticated pigment network. This work provides a solid structural basis for unravelling the mechanisms of PBS-PSII-PSI-LHC megacomplex assembly, efficient energy transfer from PBS to the two photosystems, and regulation of energy distribution between PSII and PSI.
PubMed: 36922595
DOI: 10.1038/s41586-023-05831-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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