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- W1930388675 abstract "Pigment-protein and pigment-pigment interactions are of fundamental importance to the light-harvesting and photoprotective functions essential to oxygenic photosynthesis. The orange carotenoid protein (OCP) functions as both a sensor of light and effector of photoprotective energy dissipation in cyanobacteria. We report the atomic-resolution structure of an active form of the OCP consisting of the N-terminal domain and a single noncovalently bound carotenoid pigment. The crystal structure, combined with additional solution-state structural data, reveals that OCP photoactivation is accompanied by a 12 angstrom translocation of the pigment within the protein and a reconfiguration of carotenoid-protein interactions. Our results identify the origin of the photochromic changes in the OCP triggered by light and reveal the structural determinants required for interaction with the light-harvesting antenna during photoprotection." @default.
- W1930388675 created "2016-06-24" @default.
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- W1930388675 date "2015-06-26" @default.
- W1930388675 modified "2023-10-18" @default.
- W1930388675 title "A 12 Å carotenoid translocation in a photoswitch associated with cyanobacterial photoprotection" @default.
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- W1930388675 doi "https://doi.org/10.1126/science.aaa7234" @default.
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