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Journal Article

HPr proteins of different microorganisms studied by hydrogen-1 high-resolution nuclear magnetic resonance: similarities of structures and mechanisms

MPS-Authors
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Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Hengstenberg,  Wolfgang
Max Planck Institute for Medical Research, Max Planck Society;

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Deutscher,  Josef
Max Planck Institute for Medical Research, Max Planck Society;

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https://pubs.acs.org/doi/pdf/10.1021/bi00541a012
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https://doi.org/10.1021/bi00541a012
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Citation

Kalbitzer, H. R., Hengstenberg, W., Roesch, P., Muss, P., Bernsmann, P., Engelmann, R., et al. (1982). HPr proteins of different microorganisms studied by hydrogen-1 high-resolution nuclear magnetic resonance: similarities of structures and mechanisms. Biochemistry, 21(12), 2879-2885. doi:10.1021/bi00541a012.


Cite as: https://hdl.handle.net/21.11116/0000-0005-1D40-3
Abstract
The HPr proteins of Streptococcus lactis, Streptococcus faecalis, Bacillus subtilis, and Escherichia coli were studied by 1H NMR at 360 MHz. The "active-center" histidines of all HPr proteins are characterized by a low pK value between 5.6 and 6.1 and similar spectral parameters. Phosphorylation of the histidyl residues leads to an increase of the pK value of 2-3 units 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 S. lactis is formylated at its terminal amino group.