8TO5

Central rod disk in C1 symmetry of high-resolution phycobilisome quenched by OCP (local refinement)

8TO5 の概要

• エントリーDOI: 10.2210/pdb8to5/pdb
• EMDBエントリー: 41434 41435
• 分子名称: C-phycocyanin alpha subunit, C-phycocyanin beta subunit, Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod 1, ... (6 entities in total)
• 機能のキーワード: complex, light harvesting, pigment, photosynthesis
• 由来する生物種: Synechocystis sp. PCC 6803; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 288545.32

構造登録者

Sauer, P.V.,Sutter, M.,Cupellini, L. (登録日: 2023-08-02, 公開日: 2024-04-17)

主引用文献

Sauer, 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

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

実験手法

ELECTRON MICROSCOPY (1.87 Å)