HPr proteins of different microorganisms studied by proton-high-resolution nuclear magnetic resonance: similarities of structures and mechanisms

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Abstract
The HPr proteins of Streptococcus lactis, S. faecalis, Bacillus subtilis and Escherichia coli were studied 1H NMR at 360 MHz. The active-center histidines of all HPr proteins are characterized by a low pK value betwen 5.6-6.1 and similar spectral parameters. Phosphorylation of the histidyl residues leads to an increase of the pK value of 2-3 U and spectral changes characteristic for N-1 phosphorylation of the histidyl ring. The spectra of the HPr proteins of S. lactis, S. faecalis, B. subtilis and Staphylococcus aureus reveal many similarities, whereas the spectrum of the E. coli protein is different with exception of the active-center histidine. The HPr protein of Streptococcus lactis is formylated at its terminal amino group.

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