期刊
STRUCTURE
卷 24, 期 3, 页码 448-457出版社
CELL PRESS
DOI: 10.1016/j.str.2016.01.001
关键词
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资金
- US National Science Foundation [MCB-1329956]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1623935] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [GRANTS:13895430] Funding Source: National Science Foundation
Phytochromes are photochromic photoreceptors responsible for a myriad of red/far-red light-dependent processes in plants and microorganisms. Interconversion is initially driven by photoreversible isomerization of bilin, but how this alteration directs the photostate-dependent changes within the protein to actuate signaling is poorly understood. Here, we describe the structure of the Deinococcus phytochrome photosensory module in its near complete far-red light-absorbing Pfr state. In addition to confirming the 180 degrees rotation of the D-pyrrole ring, the dimeric structure clearly identifies downstream rearrangements that trigger large-scale conformational differences between the dark-adapted and photoactivated states. Mutational analyses verified the importance of residues surrounding the bilin in Pfr stabilization, and protease sensitivity assays corroborated photostate alterations that propagate along the dimeric interface. Collectively, these data support a cooperative toggle model for phytochrome photoconversion and advance our understanding of the allosteric connection between the photosensory and output modules.
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