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Literature summary extracted from

  • Greenswag, A.R.; Muok, A.; Li, X.; Crane, B.R.
    Conformational transitions that enable histidine kinase autophosphorylation and receptor array integration (2015), J. Mol. Biol., 427, 3890-3907.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.13.3 P3P4 domain structure of Thermotoga maritima CheA, vapor diffusion method, mixing of 0.001 ml of 0.7 mM protein in 50 mM HEPES, pH 7.5, 150 mM NaCl, and 2 mM DTT, with 0.001 ml of reservoir solution containing 0.5 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 1.0 M lithium sulfate monohydrate, 4°C, X-ray small angle diffraction structure determination and analysis at 3.0 A resolution, molecular replacement and modelling Thermotoga maritima

Protein Variants

EC Number Protein Variants Comment Organism
2.7.13.3 D449A site-directed mutagenesis, the mutation in the ATP-binding pocket prevents nucleotide binding Thermotoga maritima
2.7.13.3 H405Y site-directed mutagenesis, the mutation abrogates the kinase activity Thermotoga maritima
2.7.13.3 H45K site-directed mutagenesis, a CheAFL variant that lacks the substrate His Thermotoga maritima
2.7.13.3 H45K/H405Y site-directed mutagenesis, the mutant shows reduced kinase activity compared to the wild-type Thermotoga maritima
2.7.13.3 H45K/S492C site-directed mutagenesis Thermotoga maritima
2.7.13.3 additional information disulfide cross-linking of mutant enzymes, overview Thermotoga maritima
2.7.13.3 S492C site-directed mutagenesis Thermotoga maritima

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.13.3 Mg2+ required Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.13.3 ATP + protein L-histidine Thermotoga maritima
-
 ADP + protein N-phospho-L-histidine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.13.3 Thermotoga maritima
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.13.3 phosphoprotein histidine kinase performs autophosphorylation Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.13.3 ATP + protein L-histidine
-
 Thermotoga maritima ADP + protein N-phospho-L-histidine
-
 ?
2.7.13.3 additional information histidine kinase performs autophosphorylation. The His-containing substrate domain (P1) is sequestered by interactions that depend upon P1 of the adjacent subunit. Non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility. Autophosphorylation is possible only when the subunit with a functional P4 domain trans phosphorylates a functional P1 domain of the opposing subunit Thermotoga maritima ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.13.3 CheA
-
 Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.13.3 25
-
 assay at Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.13.3 7.5
-
 assay at Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.13.3 ATP residue Ser492 resides on the ATP lid, near to the Mg2+ ion that coordinates the gamma-phosphate of ATP in the P4 active site Thermotoga maritima
2.7.13.3 additional information non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility Thermotoga maritima

General Information

EC Number General Information Comment Organism
2.7.13.3 evolution CheA differs from sensor histidine kinases in several ways: CheA does not contain a transmembrane domain, relying instead on P5 and CheW for interaction with transmembrane components. It has the phosphorylatable His residue on a separate domain (P1) instead of the dimerization domain (P3), and it utilizes a separate docking domain (P2) for CheY. P2 is not necessary for phosphotransfer to the response regulator CheY per se but variants lacking the P2 domain (DELTAP2) exhibit a reduced phosphotransfer rate relative to full-length CheA (CheAFL) and support a lower extent of chemotaxis. The linkers between the CheA domains play important roles in CheA activity Thermotoga maritima
2.7.13.3 physiological function CheA differs from sensor histidine kinases in several ways: CheA does not contain a transmembrane domain, relying instead on P5 and CheW for interaction with transmembrane components. It has the phosphorylatable His residue on a separate domain (P1) instead of the dimerization domain (P3), and it utilizes a separate docking domain (P2) for CheY. P2 is not necessary for phosphotransfer to the response regulator CheY per se but variants lacking the P2 domain (DELTAP2) exhibit a reduced phosphotransfer rate relative to full-length CheA (CheAFL) and support a lower extent of chemotaxis. The linkers between the CheA domains play important roles in CheA activity Thermotoga maritima