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Literature summary for 2.7.13.3 extracted from

  • Mechaly, A.E.; Soto Diaz, S.; Sassoon, N.; Buschiazzo, A.; Betton, J.M.; Alzari, P.M.
    Structural coupling between autokinase and phosphotransferase reactions in a bacterial histidine kinase (2017), Structure, 25, 939-944.e3 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of CpxA trapped as a hemi-phosphorylated dimer, and of the receiver domain from the response regulator partner, CpxR. The autophosphorylation of a histidine residue and the subsequent phosphoryl transfer to its response regulator CpxR can occur simultaneously, one in each protomer of the asymmetric CpxA dimer. The autokinase activity increases in the presence of phosphotransfer-impaired CpxR. In an allosteric switching mechanism, CpxR binding to one CpxA protomer may trigger autophosphorylation in the second protomer Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AE82
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Synonyms

Synonyms Comment Organism
CpxA
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Escherichia coli
sensor histidine kinase CpxA
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Escherichia coli

General Information

General Information Comment Organism
physiological function an allosteric switching mechanism may involve two autophosphorylation and two phosphotransfer reactions. The CpxR-mediated allosteric control of the autophosphorylation reaction ensures that the large-scale domain movements proceed in a coordinated way along the cycle, thus optimizing the overall catalytic efficiency Escherichia coli