Related ArticlesReexamination 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 magnetic resonance techniques has been performed, extending the work originally reported [Klevit, R. E., Drobny, G. D., & Waygood, E. B. (1986) Biochemistry 25, 7760-7769; Klevit, R. E., & Drobny, G. P. (1986) Biochemistry 25, 7770-7773; Klevit, R. E., & Waygood, E. B. (1986) Biochemistry 25, 7774-7781]. Two-dimensional homonuclear total coherence spectroscopy (TOCSY) allowed for more complete assignments of the side-chain spin systems than had been possible in the original studies. As well, two-dimensional 15N-1H heteronuclear spectroscopy was used to resolve a number of ambiguities present in the homonuclear spectra due to resonance redundancies. These analyses led to the correction of a number of resonance assignments that were made with the spectra that could be collected with the technology that existed 6 years ago. In addition, amide exchange rates and 3JNH coupling constants have been measured, extending the original analysis and yielding new structural information. All these data have been used to reexamine the folding topology of E. coli HPr. Structure calculations showed that the topology derived from the earlier NMR data, i.e., a four-stranded beta-sheet with three alpha-helices running along one side of the sheet, was essentially unchanged, although at the present level of analysis, a well-defined "helix B" could not be established with high confidence. In addition, the data reported here revealed the existence of two slowly-exchanging side-chain hydroxyl protons belonging to Ser31 and Thr59. Their behavior strongly suggests that these side chains are involved in hydrogen bonds.(ABSTRACT TRUNCATED AT 250 WORDS)
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...
nmrlearner
Journal club
0
09-30-2011 08:01 PM
[NMR paper] NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitope
NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members.
Related Articles NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members.
J Biochem. 2005 Mar;137(3):255-63
Authors: Ichikawa S, Takai T, Inoue T, Yuuki T, Okumura Y, Ogura K, Inagaki F, Hatanaka H
Group 2 major mite allergens Der f 2 and Der p 2 are classified into...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] The solution structure of the histidine-containing protein (HPr) from Staphylococcus
The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional 1H-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 The 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...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initi
Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach.
Related Articles Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach.
Science. 1993 Jun 4;260(5113):1491-6
Authors: de Dios AC, Pearson JG, Oldfield E
Recent theoretical developments permit the prediction of 1H, 13C, 15N, and 19F nuclear magnetic resonance chemical shifts in proteins and offer new ways of analyzing secondary and tertiary structure as well as for probing protein electrostatics. For 13C,...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] Characterization of tertiary interactions in a folded protein by NMR methods: studies
Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone.
Related Articles Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone.
Biochemistry. 1992 Sep 15;31(36):8587-96
Authors: Abildgaard F, Jørgensen AM, Led JJ, Christensen T, Jensen EB, Junker F, Dalbøge H
The pH-induced conformational changes in human growth hormone (hGH) have been studied, using a new...
nmrlearner
Journal club
0
08-21-2010 11:45 PM
[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...
nmrlearner
Journal club
0
08-21-2010 11:12 PM
[NMR paper] Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some i
Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics.
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 Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics.
Eur J Biochem. 1990 Nov 26;194(1):185-98
Authors: ...
nmrlearner
Journal club
0
08-21-2010 11:04 PM
[NMR paper] Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin i
Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR.
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 Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR.
Eur J Biochem. 1990 May 20;189(3):589-600
Authors: van Mierlo CP, Müller F, Vervoort J
The...