Related ArticlesSolution NMR studies on Helicobacter pylori proteins for antibiotic target discovery.
Expert Opin Drug Discov. 2016 May 23;
Authors: Lee KY, Lee BJ
Abstract
INTRODUCTION: Helicobacter pylori (H. pylori) is a well-known widespread pathogenic bacterium that survives in the extremely acidic conditions of the human gastric mucosa. The global prevalence of H. pylori-resistant antibiotics has become an emerging issue in the 21st century and has necessitated the development of novel antibiotic drugs. Many efforts have aimed to discover antibiotic target proteins of H. pylori based on its genome of more than 1600 genes.
AREAS COVERED: This article highlights NMR spectroscopy as a valuable tool for determining the structure and dynamics of potential antibiotic-targeted proteins of H. pylori and evaluating their modes of interaction with native or synthetic binding partners. The residue-specific information on binding in solution provides a structural basis to identify and optimize lead compounds.
EXPERT OPINION: NMR spectroscopy is a powerful method for obtaining details of biomolecular interactions with a broad range of binding affinities. This strength facilitates the identification of the binding interface of the encounter complex that plays an integral role in a variety of biological functions. This low-affinity complex is difficult to crystallize, which impedes structure determination using X-ray crystallography. Additionally, the relative binding affinities can be predicted from the type of spectral change upon binding. High-resolution NMR spectroscopy in combination with advanced computer simulation would provide more confidence in complex structures. The application of NMR to studies of the H. pylori protein could contribute to the development of these targeted novel antibiotics.
PMID: 27216839 [PubMed - as supplied by publisher]
[NMR paper] A few atoms make the difference: synthetic, CD, NMR and computational studies on antiviral and antibacterial activities of glycopeptide antibiotic aglycon derivatives.
A few atoms make the difference: synthetic, CD, NMR and computational studies on antiviral and antibacterial activities of glycopeptide antibiotic aglycon derivatives.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A few atoms make the difference: synthetic, CD, NMR and computational studies on antiviral and antibacterial activities of glycopeptide antibiotic aglycon derivatives.
Eur J Med Chem. 2015 Apr 13;94:73-86
Authors: Bereczki I, Mándi A, R?th E,...
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04-26-2016 12:14 PM
[NMR paper] Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.
Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.
Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.
J Biomol NMR. 2016 Mar 10;
Authors: Gardiennet C, Wiegand T, Bazin A, Cadalbert R, Kunert B, Lacabanne D, Gutsche I, Terradot L, Meier BH, Böckmann A
Abstract
We here investigate the interactions between the DnaB helicase and the C-terminal domain of the...
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03-11-2016 12:00 PM
Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori
Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori
Abstract
We here investigate the interactions between the DnaB helicase and the C-terminal domain of the corresponding DnaG primase of Helicobacter pylori using solid-state NMR. The difficult crystallization of this 387Â*kDa complex, where the two proteins interact in a six to three ratio, is circumvented by simple co-sedimentation of the two proteins directly into the MAS-NMR rotor. While the amount of information...
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03-10-2016 10:40 PM
[NMR paper] NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review.
NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review.
NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review.
Molecules. 2013;18(11):13410-24
Authors: Kang SJ, Kim DH, Lee BJ
Abstract
Due to the widespread and increasing appearance of antibiotic resistance, a new strategy is needed for developing novel antibiotics. Especially, there are no specific antibiotics for Helicobacter pylori (H. pylori). H. pylori are bacteria that live in the stomach and are...
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11-02-2013 10:04 AM
[NMR paper] NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
Related Articles NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
Biomol NMR Assign. 2013 Jul 4;
Authors: Chien CT, Wang LW, Liu YN, Hsu BD, Lyu PC, Hsu ST
Abstract
Many knotted proteins have been discovered recently, but the folding process of which remains elusive. HP0242 is a hypothetical protein from Helicobacter pylori, which is a model system for studying the folding pathway of a knotted protein. In...
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07-05-2013 09:52 PM
[NMR paper] Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Protein Expr Purif. 2013 Feb 27;
Authors: Fuengfuloy P, Chuawong P, Suebka S, Wattana-Amorn P, Williams C, Crump MP, Songsiriritthigul C
Abstract
Aminoacyl-tRNA synthetases (aaRSs) covalently...
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03-05-2013 03:25 PM
[NMR paper] The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
Dalton Trans. 2013 Jan 21;
Authors: Rowinska-Zyrek M, Potocki S, Witkowska D, Valensin D, Kozlowski H
Abstract
HypA, a nickel accessory protein from H. pylori, binds a zinc ion in it's structural site, a loop with two conserved...
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02-03-2013 10:19 AM
[NMR paper] NMR assignment of the novel Helicobacter pylori protein JHP1348.
NMR assignment of the novel Helicobacter pylori protein JHP1348.
Related Articles NMR assignment of the novel Helicobacter pylori protein JHP1348.
J Biomol NMR. 2005 Jul;32(3):262
Authors: Borin BN, Popescu A, Krezel AM
Solution NMR studies on Helicobacter pylori proteins for antibiotic target discovery.
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