Crystallization (Comment) | Organism |
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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 | UniProt | Comment | Textmining |
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Escherichia coli | P0AE82 | - |
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Synonyms | Comment | Organism |
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CpxA | - |
Escherichia coli |
sensor histidine kinase CpxA | - |
Escherichia coli |
General Information | Comment | Organism |
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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 |