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The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional ¹H-NMR spectroscopy

Kalbitzer, Hans Robert and Hengstenberg, W. (1993) The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional ¹H-NMR spectroscopy. European journal of biochemistry: EJB (= The FEBS journal) 216 (1), pp. 205-214.

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Abstract

The three-dimensional solution structure of the heat-stable phosphocarrier protein HPr from Staphylococcus aureus was determined from two-dimensional NMR data by restrained molecular dynamics. It consists of a large twisted antiparallel beta-pleated sheet with four strands A, B, C, and D of amino acids 2-7, 34-37, 40-42 and 60-65. Three right-handed helices A, B, C (amino acids 18-27, 47-53 and ...

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Item Type:Article
Date:1993
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
8365407PubMed ID
10.1111/j.1432-1033.1993.tb18134.xDOI
Classification:
NotationType
Amino Acids/chemistryMESH
Bacterial Proteins/chemistryMESH
Histidine/chemistryMESH
Magnetic Resonance SpectroscopyMESH
Phosphoenolpyruvate Sugar Phosphotransferase System/chemistryMESH
Protein ConformationMESH
Protein Structure, SecondaryMESH
Serine/chemistryMESH
Staphylococcus aureus/chemistryMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:07 Sep 2010 05:57
Last Modified:07 Sep 2010 05:57
Item ID:16479
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