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Literature summary for 2.7.13.3 extracted from

  • Sen, H.; Aggarwal, N.; Ishionwu, C.; Hussain, N.; Parmar, C.; Jamshad, M.; Bavro, V.N.; Lund, P.A.
    Structural and functional analysis of the Escherichia coli acid-sensing histidine kinase EvgS (2017), J. Bacteriol., 199, e00310 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.13.3

Crystallization (Commentary)

Crystallization (Comment) Organism
EvgS has a large periplasmic domain and a cytoplasmic PAS domain in addition to phospho-acceptor, histidine kinase and dimerization, internal receiver, and phosphotransfer domains. Homology modeling of the periplasmic region of EvgS leads to a model in which EvgS senses both external and internal pH and is activated by a shift from a tight inactive to a weak active dimer Escherichia coli

Protein Variants

Protein Variants Comment Organism
H153F mutation in periplasmic arm, mutant does not show any detectable activity above background at pH 7 or pH 5.6 Escherichia coli
H226A mutant can be induced at low pH Escherichia coli
H226L mutant cannot be induced at low pH Escherichia coli
H226N mutant cannot be induced at low pH Escherichia coli
H226Q mutant cannot be induced at low pH Escherichia coli
H226Q/S600I level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6 Escherichia coli
H226T mutant cannot be induced at low pH Escherichia coli
H226V mutant cannot be induced at low pH Escherichia coli
H226W mutant cannot be induced at low pH Escherichia coli
H63A noninducible mutant, no protein is detected Escherichia coli
H63Q/H106Q/H124Q mutations in potential His triad, mutant shows the same level of induction as the wild-type EvgS Escherichia coli
L152F/S600I level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6 Escherichia coli
additional information His226 is required for induction and is structurally colocated with Pro522 at the top of the predicted transmembrane helix. The constitutive mutations in the PAS domain can be further activated by low external pH. Expression of the cytoplasmic part of the protein alone also gives constitutive activation, which is lost if the constitutive PAS mutations are present. The cytoplasmic part shows pH-dependent dimer formation in vitro Escherichia coli
P522A/S600I level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6 Escherichia coli
S600I mutation in cytoplasmic PAS domain, renders EvgS constitutively active at pH 7 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P30855
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Synonyms

Synonyms Comment Organism
EvgS
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 Escherichia coli
sensor protein EvgS
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 Escherichia coli