Journal
STRUCTURE
Volume 23, Issue 7, Pages 1179-1189Publisher
CELL PRESS
DOI: 10.1016/j.str.2015.04.022
Keywords
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Funding
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-06CH11357]
- Michigan Technology Tri-Corridor [085P1000817]
- NIH [GM103543, GM036452, R01EY024363]
- US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- Michigan Economic Development Corporation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1413360] Funding Source: National Science Foundation
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RpBphP2 and RpBphP3, two tandem bacteriophyto-chromes from the photosynthetic bacterium Rhodopseudomonas palustris, share high sequence identity but exhibit distinct photoconversion behavior. Unlike the canonical RpBphP2, RpBphP3 photoconverts to an unusual near-red-absorbing (Pnr) state; both are required for synthesis of light-harvesting complexes under low-light conditions. Here we report the crystal structures of the photo-sensory core modules of RpBphP2 and RpBphP3. Despite different quaternary structures, RpBphP2 and RpBphP3 adopt nearly identical tertiary structures. The RpBphP3 structure reveals tongue-and-groove interactions at the interface between the GAF and PHY domains. A single mutation in the PRxSF motif at the GAF-PHY interface abolishes light-induced formation of the Pnr state in RpBphP3, possibly due to altered structural rigidity of the chromophore-binding pocket. Structural comparisons suggest that long-range signaling involves structural rearrangement of the helical spine at the dimer interface. These structures, together with mutational studies, provide insights into photoconversion and the long-range signaling mechanism in phytochromes.
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