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  Proton nuclear magnetic resonance studies on the structure and mechanism of the HPr protein of Staphylococcus aureus

Rösch, P., Kalbitzer, H. R., Schmidt-Aderjan, U., & Hengstenberg, W. (1981). Proton nuclear magnetic resonance studies on the structure and mechanism of the HPr protein of Staphylococcus aureus. Biochemistry, 20(6), 1599-1605. doi:10.1021/bi00509a029.

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Genre: Journal Article
Alternative Title : 1H nuclear magnetic resonance studies on the structure and mechanism of the HPr protein of Staphylococcus aureus

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 Creators:
Rösch, Paul1, Author              
Kalbitzer, Hans Robert1, Author              
Schmidt-Aderjan, Ulrike2, Author              
Hengstenberg, Wolfgang2, Author              
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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: 1H NMR studies of the phosphocarrier protein HPr and its three nitrotyrosyl derivatives revealed some structural features which may finally lead to an explanation of the mechanism of the phospho-transfer reaction. Titration studies on mononitrated, dinitrated, and trinitrated derivatives--i.e., derivatives with Tyr-56, Tyr-56 and Tyr-37, and Tyr-56, Tyr-37, and Tyr-6 modified--have been performed. The three tyrosyl residues seem to be in positions completely different from each other with respect to their solvent accessibility; Tyr-56 seems to be located near the surface of the protein, Tyr-6 seems to be completely buried, and Tyr-37 takes an intermediate position. Tyr-6 contributes to the core structure of the protein. A resonance at -0.18 ppm could be shown to correspond to a CH3 group of a valine. Nuclear Overhauser experiments revealed its being close to Tyr-6. One of the resonances tentatively assigned to methionine SCH3 groups titrates in the dinitrated derivative with the same pK as nitrotyrosyl residue 37. The titration behavior of the active-center histidyl residue suggests a hydrogen bond to the imidazole ring, possibly from Tyr-56 or Arg-17.

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Language(s): eng - English
 Dates: 1980-09-251981-03-01
 Publication Status: Published in print
 Pages: 7
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 Rev. Type: Peer
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 20 (6) Sequence Number: - Start / End Page: 1599 - 1605 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103