Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs

Mitchell Brüderlin, Raphael Böhm, Firas Fadel, Sebastian Hiller, Tilman Schirmer () and Badri N. Dubey ()
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Mitchell Brüderlin: University of Basel
Raphael Böhm: University of Basel
Firas Fadel: University of Basel
Sebastian Hiller: University of Basel
Tilman Schirmer: University of Basel
Badri N. Dubey: University of Basel

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: Abstract In two-component systems, the information gathered by histidine kinases (HKs) are relayed to cognate response regulators (RRs). Thereby, the phosphoryl group of the auto-phosphorylated HK is transferred to the receiver (Rec) domain of the RR to allosterically activate its effector domain. In contrast, multi-step phosphorelays comprise at least one additional Rec (Recinter) domain that is typically part of the HK and acts as an intermediary for phosphoryl-shuttling. While RR Rec domains have been studied extensively, little is known about discriminating features of Recinter domains. Here we study the Recinter domain of the hybrid HK CckA by X-ray crystallography and NMR spectroscopy. Strikingly, all active site residues of the canonical Rec-fold are pre-arranged for phosphoryl-binding and BeF3- binding does not alter secondary or quaternary structure, indicating the absence of allosteric changes, the hallmark of RRs. Based on sequence-covariation and modeling, we analyze the intra-molecular DHp/Rec association in hybrid HKs.

Date: 2023
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DOI: 10.1038/s41467-023-36597-8

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