期刊
SCIENCE
卷 348, 期 6242, 页码 1463-1466出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaa7234
关键词
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资金
- U.S. Department of Energy (DOE), Basic Energy Sciences [DE-FG02-91ER20021]
- Office of Science, Office of Basic Energy Sciences, of the U.S. DOE [DE-AC02-05CH11231]
- Office of Science of the U.S. DOE [DE-AC02-05CH11231]
- Office of Science, Office of Biological and Environmental Research, of the U.S. DOE [DE-AC02-05CH11231]
- Agence Nationale de la Recherche (ANR, project CYANOPROTECT)
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.
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