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Crystal structure of a fluorescence optimized bathy phytochrome PAiRFP2 derived from wild-type Agp2 in its functional Meta-F intermediate state.Crystal structure of a fluorescence optimized bathy phytochrome PAiRFP2 derived from wild-type Agp2 in its functional Meta-F intermediate state.
Structural highlights
FunctionPublication Abstract from PubMedPhytochromes are modular photoreceptors of plants, bacteria and fungi that use light as a source of information to regulate fundamental physiological processes. Interconversion between the active and inactive states is accomplished by a photoinduced reaction sequence which couples the sensor with the output module. However, the underlying molecular mechanism is yet not fully understood due to the lack of structural data of functionally relevant intermediate states. Here we report the crystal structure of a Meta-F intermediate state of an Agp2 variant from Agrobacterium fabrum. This intermediate, the identity of which was verified by resonance Raman spectroscopy, was formed by irradiation of the parent Pfr state and displays significant reorientations of almost all amino acids surrounding the chromophore. Structural comparisons allow identifying structural motifs that might serve as conformational switch for initiating the functional secondary structure change that is linked to the (de-)activation of these photoreceptors. Structural snapshot of a bacterial phytochrome in its functional intermediate state.,Schmidt A, Sauthof L, Szczepek M, Lopez MF, Escobar FV, Qureshi BM, Michael N, Buhrke D, Stevens T, Kwiatkowski D, von Stetten D, Mroginski MA, Krauss N, Lamparter T, Hildebrandt P, Scheerer P Nat Commun. 2018 Nov 21;9(1):4912. doi: 10.1038/s41467-018-07392-7. PMID:30464203[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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