8to2
From Proteopedia
Bottom cylinder of high-resolution phycobilisome quenched by OCP (local refinement)
Structural highlights
Publication Abstract from PubMedCyanobacteria 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. Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes.,Sauer PV, Cupellini L, Sutter M, Bondanza M, Dominguez Martin MA, Kirst H, Bina D, Koh AF, Kotecha A, Greber BJ, Nogales E, Polivka T, Mennucci B, Kerfeld CA Sci Adv. 2024 Apr 5;10(14):eadk7535. doi: 10.1126/sciadv.adk7535. Epub 2024 Apr , 5. PMID:38578996[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|