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

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0005-1D40-3 Version Permalink: https://hdl.handle.net/21.11116/0000-0005-1D41-2
Genre: Journal Article

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Biochem_21_1982_2879.pdf (Any fulltext), 849KB
 
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https://pubs.acs.org/doi/pdf/10.1021/bi00541a012 (Any fulltext)
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 Creators:
Kalbitzer, Hans Robert1, Author           
Hengstenberg, Wolfgang2, Author           
Roesch, P., Author
Muss , P. , Author
Bernsmann, P., Author
Engelmann, R., Author
Doerschug, M., Author
Deutscher, Josef2, Author           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 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.

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Language(s): eng - English
 Dates: 1981-08-261982-06-08
 Publication Status: Issued
 Pages: 7
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi00541a012
URI: https://www.ncbi.nlm.nih.gov/pubmed/6809041
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 21 (12) Sequence Number: - Start / End Page: 2879 - 2885 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103