8f71

Crystal structure of the histidine kinase domain of bacteriophytochrome RpBphP2

spinqualitylabelsall models 8f71, resolution 3.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8f71 is a 2 chain structure with sequence from Rhodopseudomonas palustris CGA009. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.19Å Ligands: ATP, MG, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6N5G3_RHOPA Publication Abstract from PubMed Phytochromes are red-light photoreceptors that regulate a wide range of physiological processes in plants, fungi and bacteria. Canonical bacteriophytochromes are photosensory histidine kinases that undergo light-dependent autophosphorylation, thereby regulating cellular responses to red light via two-component signaling pathways. However, the molecular mechanism of kinase activation remains elusive for bacteriophytochromes. In particular, the directionality of autophosphorylation is still an open question in these dimeric photoreceptor kinases. In this work, we perform histidine kinase assays on two tandem bacteriophytochromes RpBphP2 and RpBphP3 from the photosynthetic bacterium Rhodopseudomonas palustris. By examining the kinase activities of full-length bacteriophytochromes and two loss-of-function mutants under different light conditions, we demonstrate that RpBphP2 and RpBphP3 undergo light-dependent trans-phosphorylation between protomers in both homodimeric and heterodimeric forms. We have further determined the crystal structure of the histidine kinase domains of RpBphP2 at 3.19 A resolution. Based on structural comparisons and homology modeling, we also present a model to account for the actions of trans-autophosphorylation in bacteriophytochromes. Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.,Kumarapperuma I, Tom IP, Bandara S, Montano S, Yang X Photochem Photobiol Sci. 2023 Jun;22(6):1257-1266. doi: , 10.1007/s43630-023-00366-9. Epub 2023 Feb 9. PMID:36757561 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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