6TNE

Crystal structure of receiver domain from Hybrid Histidine Kinase CckA

Summary for 6TNE

• Entry DOI: 10.2210/pdb6tne/pdb
• Descriptor: Histidine kinase (2 entities in total)
• Functional Keywords: cyclic di-gmp, second messenger, hybride histidine kinase, ccka, phosphorylation, transferase
• Biological source: Caulobacter vibrioides
• Total number of polymer chains: 1
• Total formula weight: 12958.78

Authors

Dubey, B.N.,Bruederlin, M.,Schirmer, T. (deposition date: 2019-12-06, release date: 2020-12-16, Last modification date: 2025-09-10)

Primary citation

Bruderlin, M.,Bohm, R.,Fadel, F.,Hiller, S.,Schirmer, T.,Dubey, B.N.
Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs.
Nat Commun, 14:1002-1002, 2023

PubMed 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 (Rec) 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 Rec domains. Here we study the Rec 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 BeF 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.

PubMed: 36864019
DOI: 10.1038/s41467-023-36597-8

Experimental method

X-RAY DIFFRACTION (1.25 Å)