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Literature summary for 2.7.13.3 extracted from

  • Moore, J.O.; Hendrickson, W.A.
    Structural analysis of sensor domains from the TMAO-responsive histidine kinase receptor TorS (2009), Structure, 17, 1195-1204.
    View publication on PubMed
Search for more literature for 2.7.13.3

Cloned(Commentary)

Cloned (Comment) Organism
cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells Vibrio parahaemolyticus
cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, at 4°C against a buffer containing 5%–10% (v/v) 1-4 butanediol, 0.1 M Na-aetate (pH 5.5), 25–100 mM NH4SO4 Escherichia coli
hanging drop vapor diffusion method, at 4°C against a buffer containing 7%–13% (w/v) PEG 4000, 0.1 M Tris (pH 7.5) Vibrio parahaemolyticus

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
 gel filtration Escherichia coli
75000
-
 gel filtration Vibrio parahaemolyticus

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli P39453
-
-
Vibrio parahaemolyticus
-
-
-
Vibrio parahaemolyticus EB101
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap Ni2+-chelating column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration Vibrio parahaemolyticus
HiTrap Ni2+-chelating column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration Escherichia coli

Source Tissue

Source Tissue Comment Organism Textmining

Subunits

Subunits Comment Organism
dimer the isolated TorS sensor domain dimerizes in solution Escherichia coli
dimer the isolated TorS sensor domain dimerizes in solution Vibrio parahaemolyticus

Synonyms

Synonyms Comment Organism
TMAO reductase S
-
 Vibrio parahaemolyticus
TMAO reductase S
-
 Escherichia coli
TorS
-
 Escherichia coli
TorS
-
 Vibrio parahaemolyticus
TorS a sensor histidine kinase Vibrio parahaemolyticus
TorS sensor histidine kinase Escherichia coli
trimethylamine-N-oxide reductase S
-
 Vibrio parahaemolyticus
trimethylamine-N-oxide reductase S
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the TorS histidine kinase activates the trimethylamine-N-oxide reductase pathway when sensing trimethylamine-N-oxide in the environment Escherichia coli
physiological function the TorS histidine kinase activates the trimethylamine-N-oxide reductase pathway when sensing trimethylamine-N-oxide in the environment Vibrio parahaemolyticus