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bioRxiv · 10.1101/2021.11.15.468719

Structure of the Quenched Cyanobacterial OCP-Phycobilisome Complex

Dominguez-Martin, M. A.·Sauer, P. V.·Sutter, M.·Kirst, H.·Bina, D.·Greber, B. J.·Nogales, E.·Polivka, T.·Kerfeld, C. A.
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Abstract

Photoprotection is an essential mechanism in photosynthetic organisms to balance the harvesting of light energy against the risks of photodamage. In cyanobacteria, photoprotective non-photochemical quenching relies on the interaction between a photoreceptor, the Orange Carotenoid Protein (OCP), and the antenna, the phycobilisome (PBS). Here we report the first structure of the OCP-PBS complex at 2.7 [A] overall resolution obtained by cryo-electron microscopy. The structure shows that the 6.2 MDa PBS is quenched by four 34 kDa OCP organized as two dimers. The complex also reveals that the structure of the active form of the OCP is drastically different than its resting, non-quenching form, with an [~]60 [A] displacement of its regulatory domain. These results provide a high-resolution blueprint of the structural basis of the protective quenching of excess excitation energy that enables cyanobacteria to harvest light energy and fix CO2 across environmentally diverse and dynamic surface of our planet.

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Dominguez-Martin, M. A., Sauer, P. V., Sutter, M., Kirst, H., Bina, D., Greber, B. J., Nogales, E., Polivka, T., Kerfeld, C. A.. 2021-11-15. Structure of the Quenched Cyanobacterial OCP-Phycobilisome Complex. https://doi.org/10.1101/2021.11.15.468719

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