Fig. 4: Comparison of DrBphP-DrRR in Pr (blue) and Pfr (magenta) reveals a zipper-like opening at the neck.
From: Structural mechanism of signal transduction in a phytochrome histidine kinase
a The entire structure is compared. The CA domains in the Pr-state structure are shown as transparent. They were not refined against the data and are taken from a homology model against the structure of a histidine kinase from Thermotoga maritima (pdb entry 2C2A)52. The black dots indicate the center of mass of the PHY domains. b The graph shows the distance between Cα atoms across the dimer interface in the neck region. Source data are provided as a Source Data file. c The neck region with the densities is shown for Pr (blue) and Pfr (magenta). A zipper-like opening of the dimerization interface is observed. The insets show detailed interactions between sister residues Ser519 and Asn520 (upper), Asn513 (middle), and Leu502, Leu506 and Ile509 (lower). The structures are colored according to their state, the hydrogen bonds are shown in yellow dashed lines, and the distances are in Å.
