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7Y4L

PBS of PBS-PSII-PSI-LHCs from Porphyridium purpureum.

This is a non-PDB format compatible entry.
Summary for 7Y4L
Entry DOI10.2210/pdb7y4l/pdb
EMDB information33605
DescriptorLinker4, Phycobilisome 31.8 kDa linker polypeptide, phycoerythrin-associated, rod, Phycobilisome 27.9 kDa linker polypeptide, phycoerythrin-associated, rod, ... (33 entities in total)
Functional Keywordspbs, photosynthesis
Biological sourcePorphyridium purpureum
More
Total number of polymer chains716
Total formula weight15003494.12
Authors
You, X.,Zhang, X.,Cheng, J.,Xiao, Y.N.,Sun, S.,Sui, S.F. (deposition date: 2022-06-15, release date: 2023-01-18, Last modification date: 2023-04-19)
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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