Fig. 4: Possible model of the PsBphP1 dimer as Pfr based on cryo-EM maps of the DoD. | Nature Communications

Fig. 4: Possible model of the PsBphP1 dimer as Pfr based on cryo-EM maps of the DoD.

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

Fig. 4

Shown are orthogonal views of the PsBphP1 dimer either alone or superposed with a cryo-EM composite map of the region derived from the full-length DoD map and a focused refinement map of the DoD contacts at the HK bidomain (see Supplementary Figs. 5 and 10). The dark gray surface delineates one dimer, while EM density for the opposing dimer was rendered as a white surface. Domains and features are colored as in Fig. 2. His530 is shown in red spheres. ATP-binding pocket of the CA domain in the A protomer is outlined with a dashed black circle. The dashed red circles locate the CA domain from the B protomer, which was added in an arbitrary orientation for completeness, but is absent in the EM density map. As seen in Supplementary Fig. 10, EM density dissipates at the terminus of helix α2 of the DHp domain of protomer B.

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