Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.13.3 extracted from

  • Gudipaty, S.A.; McEvoy, M.M.
    The histidine kinase CusS senses silver ions through direct binding by its sensor domain (2014), Biochim. Biophys. Acta, 1844, 1656-1661.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene cusS, recombinant expression of the enzyme's periplasmic domain from pTXB3CusSs plasmid, encoding CusS amino acids 39-187 with a chitin binding domain (CBD) affinity tag, in Escherichia coli strain BL21(DE3) Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane a periplasmic sensor domain is flanked by transmembrane alpha-helices which link it to conserved cytoplasmic catalytic domains Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ag+ the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. No molecules of Ag+ per enzyme molecule for the purified enzyme, and 3.82 molecules of Ag+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions Escherichia coli
Cu+ 0.14 molecules of Cu+ per enzyme molecule for the purified enzyme, and 0.23 molecules of Cu+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions Escherichia coli
additional information the enzyme does not bind Ni2+ or Zn2+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
CusSs samples for analytical ultracentrifugation experiments are prepared by dialysis against 5fold molar excesses of AgNO3, ZnCl2 or NiCl2 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P77485 W3110
-

Purification (Commentary)

Purification (Comment) Organism
recombinant CBD-tagged enzyme from Escherichia coli strain BL21(DE3) by chitin affinity chromatography with DTT thiol-induced cleavage and gel filtration to over 95% purity Escherichia coli

Subunits

Subunits Comment Organism
dimer periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize Escherichia coli
More CusS is predicted to be a canonical histidine kinase with a periplasmic sensor domain connected by transmembrane helices to the catalytic cytoplasmic domains Escherichia coli

Synonyms

Synonyms Comment Organism
CusS
-
Escherichia coli

General Information

General Information Comment Organism
evolution the CusS histidine kinase has overall sequence identity to putative metal-sensing HKs such as SilS (56%), CopS (42%), PcoS (38%) and CinS (35%) Escherichia coli
additional information the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. For NMR structure analysis, the enzyme is prepared with Ag+, Ni2+, Zn2+, and Cu+ ions via dialysis Escherichia coli
physiological function CusS is a prototypical periplasmic sensing histidine kinase, the histidine kinase CusS of the CusRS two-component system functions as a Ag(I)/Cu(I)-responsive sensor kinase and is essential for induction of the genes encoding the CusCFBA efflux pump. CusS has an important role in silver resistance and regulation of copper homeostasis Escherichia coli