Related ArticlesThe solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional 1H-NMR spectroscopy.
Eur J Biochem. 1993 Aug 15;216(1):205-14
Authors: Kalbitzer HR, Hengstenberg W
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 71-85) are positioned on top of this sheet. The aromatic ring of His15 is located in a cleft formed by amino acids 12-17 and 55-58, only the nitrogen (N delta 1) atom which can be phosphorylated by enzyme I is exposed to the water. The side chains of Thr12 and Arg17 are located close to the histidine ring. The regulatory serine residue (Ser46) is located in a hydrophobic patch, its hydroxyl group is water-accessible but forms hydrogen bonds with the amide groups of the backbone. The general features of the three-dimensional structure are similar to those found in HPr proteins from different microorganisms such as Escherichia coli, Bacillus subtilis and Streptococcus faecalis.
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
Abstract The bacterial histidine autokinase CheA contains a histidine phosphotransfer (Hpt) domain that accepts a phosphate from the catalytic domain and donates the phosphate to either target response regulator protein, CheY or CheB. The Hpt domain forms a helix-bundle structure with a conserved four-helix bundle motif and a variable fifth helix. Observation of two nearly equally populated conformations in the crystal...
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[NMR paper] 15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnos
15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure.
Related Articles 15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure.
Protein Sci. 2000 Apr;9(4):693-703
Authors: Kalbitzer HR, Görler A, Li H, Dubovskii PV, Hengstenberg W, Kowolik C, Yamada H, Akasaka K
The pressure-induced changes in 15N enriched HPr from Staphylococcus carnosus were investigated by two-dimensional (2D) heteronuclear NMR spectroscopy at pressures ranging from...
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[NMR paper] NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ.
NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ.
Related Articles NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ.
Nature. 1998 Nov 5;396(6706):88-92
Authors: Tanaka T, Saha SK, Tomomori C, Ishima R, Liu D, Tong KI, Park H, Dutta R, Qin L, Swindells MB, Yamazaki T, Ono AM, Kainosho M, Inouye M, Ikura M
Bacteria live in capricious environments, in which they must continuously sense external conditions in order to adjust their shape, motility and physiology. The histidine-aspartate...
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[NMR paper] Determination of the three-dimensional solution structure of the histidine-containing
Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy.
Eur J Biochem. 1992 Dec 15;210(3):881-91
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[NMR paper] Reexamination of the secondary and tertiary structure of histidine-containing protein
Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.
Related Articles Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.
Biochemistry. 1991 Dec 24;30(51):11842-50
Authors: Hammen PK, Waygood EB, Klevit RE
Analysis of the histidine-containing protein (HPr) from Escherichia coli by two-dimensional homonuclear and heteronuclear nuclear...
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[NMR paper] Reexamination of the secondary and tertiary structure of histidine-containing protein
Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.
Related Articles Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.
Biochemistry. 1991 Dec 24;30(51):11842-50
Authors: Hammen PK, Waygood EB, Klevit RE
Analysis of the histidine-containing protein (HPr) from Escherichia coli by two-dimensional homonuclear and heteronuclear nuclear...
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[NMR paper] Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete se
Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Related Articles Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Biochemistry. 1991 Nov 19;30(46):11186-92
Authors: Kalbitzer HR, Neidig KP, Hengstenberg W
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure...
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[NMR paper] Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete se
Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Related Articles Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Biochemistry. 1991 Nov 19;30(46):11186-92
Authors: Kalbitzer HR, Neidig KP, Hengstenberg W
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure...