Fig. 2: Maps of P. syringae (Ps) BphP1 as Pr shown in low contour inform the relative positions of the S-helices and HK bidomains in the dimer. | Nature Communications

Fig. 2: Maps of P. syringae (Ps) BphP1 as Pr shown in low contour inform the relative positions of the S-helices and HK bidomains in the dimer.

From: Signaling by a bacterial phytochrome histidine kinase involves a conformational cascade reorganizing the dimeric photoreceptor

Fig. 2

a Orthogonal cartoon views of full-length PsBphP1 as Pr (PDB 8U8Z) modeled from a 3.5-Å resolution map that allowed extension of the structure into the S-helix/DHp regions connecting the PSMs to the HK bidomains. Color scheme is the same as in Fig. 1d, with the purple coloring added for the DHp domains. His530 predicted to participate in the HK phosphorelay is shown as red spheres. b An unsharpened EM density map of full-length PsBphP1 contoured at 2 σ reveals a more complete dimer. c Positioning of the protomers as cartoon models in the map from (b) showing the relative positions of the PSM and HK regions. The position of the loop between the Hα1 and Hα2 regions of the DHp domains was extended from those in (a) using the predicted AlphaFold structure of PsBphP1 (AF-Q885D3-F1). In the absence of sufficiently resolved CA domains, we docked a predicted cartoon model (shown in magenta) of the CA domain developed in RoseTTA-fold34. ATP-binding pocket in the CA domains is outlined by the dashed black ovals. d Orthogonal cartoon views of a predicted model for the DHp domains superposed with an unsharpened map of PsBphP1 as Pr (gray mesh) contoured at 4 σ. The S-helix is colored in teal/light cyan and the DHp domains in purple. His530 is shown as red spheres. The CA domains were omitted for clarity.

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