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8TRO

Rod from high-resolution phycobilisome quenched by OCP (local refinement)

This is a non-PDB format compatible entry.
Summary for 8TRO
Entry DOI10.2210/pdb8tro/pdb
EMDB information41434 41435 41436 41585
DescriptorC-phycocyanin alpha subunit, C-phycocyanin beta subunit, Phycobilisome rod-core linker polypeptide CpcG, ... (8 entities in total)
Functional Keywordscomplex, light harvesting, pigment, photosynthesis
Biological sourceSynechocystis sp. PCC 6803
More
Total number of polymer chains40
Total formula weight777118.17
Authors
Sauer, P.V.,Sutter, M.,Cupellini, L. (deposition date: 2023-08-09, release date: 2024-04-17)
Primary citationSauer, P.V.,Cupellini, L.,Sutter, M.,Bondanza, M.,Dominguez Martin, M.A.,Kirst, H.,Bina, D.,Koh, A.F.,Kotecha, A.,Greber, B.J.,Nogales, E.,Polivka, T.,Mennucci, B.,Kerfeld, C.A.
Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes.
Sci Adv, 10:eadk7535-eadk7535, 2024
Cited by
PubMed Abstract: Cyanobacteria use large antenna complexes called phycobilisomes (PBSs) for light harvesting. However, intense light triggers non-photochemical quenching, where the orange carotenoid protein (OCP) binds to PBS, dissipating excess energy as heat. The mechanism of efficiently transferring energy from phycocyanobilins in PBS to canthaxanthin in OCP remains insufficiently understood. Using cryo-electron microscopy, we unveiled the OCP-PBS complex structure at 1.6- to 2.1-angstrom resolution, showcasing its inherent flexibility. Using multiscale quantum chemistry, we disclosed the quenching mechanism. Identifying key protein residues, we clarified how canthaxanthin's transition dipole moment in its lowest-energy dark state becomes large enough for efficient energy transfer from phycocyanobilins. Our energy transfer model offers a detailed understanding of the atomic determinants of light harvesting regulation and antenna architecture in cyanobacteria.
PubMed: 38578996
DOI: 10.1126/sciadv.adk7535
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (1.9 Å)
Structure validation

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