The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
J Biol Chem. 2003 Oct 3;278(40):39185-8
Authors: Pappalardo L, Janausch IG, Vijayan V, Zientz E, Junker J, Peti W, Zweckstetter M, Unden G, Griesinger C
The structure of the water-soluble, periplasmic domain of the fumarate sensor DcuS (DcuS-pd) has been determined by NMR spectroscopy in solution. DcuS is a prototype for a sensory histidine kinase with transmembrane signal transfer. DcuS belongs to the CitA family of sensors that are specific for sensing di- and tricarboxylates. The periplasmic domain is folded autonomously and shows helices at the N and the C terminus, suggesting direct linking or connection to helices in the two transmembrane regions. The structure constitutes a novel fold. The nearest structural neighbor is the Per-Arnt-Sim domain of the photoactive yellow protein that binds small molecules covalently. Residues Arg107, His110, and Arg147 are essential for fumarate sensing and are found clustered together. The structure constitutes the first periplasmic domain of a two component sensory system and is distinctly different from the aspartate sensory domain of the Tar chemotaxis sensor.
Metabolic characterization of Palatinate German white wines according to sensory attributes, varieties, and vintages using NMR spectroscopy and multivariate data analyses
Metabolic characterization of Palatinate German white wines according to sensory attributes, varieties, and vintages using NMR spectroscopy and multivariate data analyses
Abstract 1H NMR (nuclear magnetic resonance spectroscopy) has been used for metabolomic analysis of â??Rieslingâ?? and â??Mueller-Thurgauâ?? white wines from the German Palatinate region. Diverse two-dimensional NMR techniques have been applied for the identification of metabolites, including phenolics. It is shown that sensory analysis correlates with NMR-based metabolic profiles of wine. 1H NMR data in combination...
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[NMR paper] The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining pro
The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining protein structure prediction methods with NMR spectroscopy.
Related Articles The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining protein structure prediction methods with NMR spectroscopy.
J Magn Reson. 2005 Apr;173(2):310-6
Authors: Meiler J, Baker D
We illustrate how moderate resolution protein structures can be rapidly obtained by interlinking computational prediction methodologies with un- or partially assigned NMR data. To...
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Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
Related Articles Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
J Am Chem Soc. 2010 Aug 20;
Authors: Hu Y, Zhao E, Li H, Xia B, Jin C
The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive...
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[NMR paper] Solution structure of phenol hydroxylase protein component P2 determined by NMR spect
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
Biochemistry. 1997 Jan 21;36(3):495-504
Authors: Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the...
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[NMR paper] Solution structure of phenol hydroxylase protein component P2 determined by NMR spect
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
Biochemistry. 1997 Jan 21;36(3):495-504
Authors: Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the...
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[NMR paper] RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprote
RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2495-9
Authors: Hoffman DW, Query CC, Golden BL, White...
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[NMR paper] Solution structure of component B from methane monooxygenase derived through heteronu
Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
Biochemistry. 1999 May 4;38(18):5799-812
Authors: Chang SL, Wallar BJ, Lipscomb JD, Mayo KH
Methane monooxygenase (MMO) is a nonheme iron-containing enzyme which consists of three protein components: a...
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Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis
Yunfei Hu et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1053785/aop/images/medium/ja-2010-053785_0001.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society
The NMR structure of the sensory domain of the membranous two-component fumarate sens
Linear Mode
