The Signaling Pathway in Histidine Kinase and the Response Regulator Complex Revealed by X-ray Crystallography and Solution Scattering

Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation

“…S4), multiple signs suggest a conserved signaling mode through the β-sheet in these domains. It is also worth noting that this LOV/DHpL interaction also seems to occlude the area known to contain the residues that mediate interaction between HK and RR (17,18), suggesting that the LOV domain might also play a role in regulation at the level of phosphotransfer and/or phosphatase activity.…”

Small-Angle X-ray Scattering Reveals the Solution Structure of a Bacteriophytochrome in the Catalytically Active Pr State

“…These suggest some flexibility in the CA domains with envelops larger than are required although it is difficult to say if there is more than one CA domain conformation. Low-resolution X-ray (4.2 Å) and SAXS structures have been reported, 29 of a histidine kinase in complex with a response regulator (RR), that show the RR attached to the catalytic His. The overall shape, of the SAXS ab initio model, is very similar to the C terminal half of the model proposed here, with the difference that a CA domain takes the place of the RR.…”

The Structure of the KinA-Sda Complex Suggests an Allosteric Mechanism of Histidine Kinase Inhibition

“…A similar extended arrangement of CA and DHp domains is noted in a model derived from low resolution X-ray diffraction and small-angle X-ray scattering of the ThkA-TrrA HK-RR complex from T. maritima. 14 Two molecules of Sda bind to a dimer of KinA (KinA 2 ), to form a KinA 2 -2Sda heterotetramer, and in doing so increase the stability of the KinA 2 . 4 Whilst a combination of site-directed mutagenesis, pull-down and kinase assays identified the surface of Sda involved with binding KinA, little is known of the molecular surface of KinA to which Sda binds.…”