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Literature summary for 2.7.13.3 extracted from

  • Rinaldi, J.; Arrar, M.; Sycz, G.; Cerutti, M.L.; Berguer, P.M.; Paris, G.; Estrin, D.A.; Marti, M.A.; Klinke, S.; Goldbaum, F.A.
    Structural insights into the HWE histidine kinase family: the Brucella blue light-activated histidine kinase domain (2016), J. Mol. Biol., 428, 1165-1179.
    View publication on PubMed
Search for more literature for 2.7.13.3

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzyme domains in Escherichia coli strain BL21(DE3) Brucella sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
Brucella LOV-HK histidine kinase domain free or in complex with non-hydrolyzable ATP analogue AMP-PCP, mixing of 1 mg/ml protein in 50 mM MES, pH 6.5, and 250 mM sodium chloride, with precipitation solution, X-ray diffraction structure determination and analysis at 2.51 A resolution, molecular modeling Brucella sp.

Protein Variants

Protein Variants Comment Organism
A287C/L333C site-directed mutagenesis, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme Brucella sp.
I286C site-directed mutagenesis of the long HK domain version, the mutation is located in the alpha1 helix N-terminal to the histidine phosphoacceptor, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme Brucella sp.
I286C/N388A site-directed mutagenesis of the short HK domain version, the N388A mutation impairs the phosphorylation capacity, the mutant is unable to bind ATP Brucella sp.
additional information generation of two different versions of the HK domain: one long (L, the HK domain plus a 23-kDa tag, 49 kDa) and other short (S, 26 kDa). The short version has the N388A mutation which impairs the phosphorylation capacity. Both versions have the I286C mutation Brucella sp.
V282C site-directed mutagenesis, the mutation is located in the alpha1 helix N-terminal to the histidine phosphoacceptor, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme Brucella sp.

General Stability

General Stability Organism
DTT stabilizes Brucella sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Brucella sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + protein L-histidine Brucella sp.
-
 ADP + protein N-phospho-L-histidine
-
 ?

Organism

Organism UniProt Comment Textmining
Brucella sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzyme domains from Escherichia coli strain BL21(DE3) by ultracentrifugation, nickel affinity chromatography, dialysis, and gel filtration Brucella sp.

Reaction

Reaction Comment Organism Reaction ID
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine catalytic mechanism for Brucella LOV-HK, molecular modeling and simulations, overview Brucella sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + protein L-histidine
-
 Brucella sp. ADP + protein N-phospho-L-histidine
-
 ?
additional information autophosphorylation occurs when the ATP molecule bound to the the catalytic and ATP-binding subdomain phosphorylates the histidine residue in the dimerization/histidine phosphoacceptor subdomain. Histidine kinase dimerization implies that the directionality of the autophosphorylation reaction can proceed either in a cis (intramolecular) or in a trans (intermolecular) manner. Autophosphorylation occurs in cis in the dimer. Intramolecular interactions in the enzyme, overview. Arg321 from the alpha2 helix of the dimerization/histidine phosphoacceptor subdomain contacts Glu384, Tyr383 and the gamma phosphate from non-hydrolyzable ATP analogue AMP-PCP, closing the binding pocket Brucella sp. ?
-
 ?

Subunits

Subunits Comment Organism
dimer the Brucella HK domain presents two different dimeric assemblies in the asymmetric unit: one similar to canonical parallel homodimers (C) and the other, an antiparallel non-canonical (NC) dimer, each with distinct relative subdomain orientations and dimerization interfaces. The C dimer is the functionally relevant species and can be stabilized and is active in solution. The HK domain is a monomer in solution and presents autokinase activity Brucella sp.
More Brucella LOV-HK comprises an N-terminal blue-light sensor (LOV) domain, followed by a central PAS domain and a C-terminal HK domain. Crystal structure analysis, overview Brucella sp.

Synonyms

Synonyms Comment Organism
light-activated histidine kinase
-
 Brucella sp.
LOV-HK
-
 Brucella sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Brucella sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Brucella sp.

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Brucella sp.

General Information

General Information Comment Organism
evolution the Brucella histidine kinase domain belongs to the HWE histidine kinase family. The HWE HK domains are present in LOV-HKs and bacteriophytochromes among other proteins Brucella sp.
additional information the HK domain is a monomer in solution and presents autokinase activity Brucella sp.
physiological function in response to light, as part of a two-component system, the Brucella blue light-activated histidine kinase (LOV-HK) increases its autophosphorylation, modulating the virulence of this microorganism Brucella sp.