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 related to many serious gastric problems such as peptic ulcers, chronic gastritis, mucosa-associated lymphoid tissue lymphoma, and gastric cancer. Because of its importance as a human pathogen, it's worth studying the structure and function of the proteins from H. pylori. After the sequencing of the H. pylori strain 26695 in 1997, more than 1,600 genes were identified from H. pylori. Until now, the structures of 334 proteins from H. pylori have been determined. Among them, 309 structures were determined by X-ray crystallography and 25 structures by Nuclear Magnetic Resonance (NMR), respectively. Overall, the structures of large proteins were determined by X-ray crystallography and those of small proteins by NMR. In our lab, we have studied the structural and functional characteristics of small proteins from H. pylori. In this review, 25 NMR structures of H. pylori proteins will be introduced and their structure-function relationships will be discussed.
[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] Sliding and target location of DNA-binding proteins:an NMR view of the lac repressor system.
Sliding and target location of DNA-binding proteins:an NMR view of the lac repressor system.
Related Articles Sliding and target location of DNA-binding proteins:an NMR view of the lac repressor system.
J Biomol NMR. 2013 Apr 9;
Authors: Loth K, Gnida M, Romanuka J, Kaptein R, Boelens R
Abstract
In non-specific lac headpiece-DNA complexes selective NMR line broadening is observed that strongly depends on length and composition of the DNA fragments. This broadening involves amide protons found in the non-specific lac-DNA structure to be...
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04-10-2013 07:21 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
Packing Interactions inHydrated and Anhydrous Formsof the Antibiotic Ciprofloxacin: a Solid-State NMR, X-ray Diffraction,and Computer Simulation Study
Packing Interactions inHydrated and Anhydrous Formsof the Antibiotic Ciprofloxacin: a Solid-State NMR, X-ray Diffraction,and Computer Simulation Study
Lui?s Mafra, Se?rgio M. Santos, Rene?e Siegel, Ine?s Alves, Filipe A. Almeida Paz, Dmytro Dudenko and Hans W. Spiess
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja208647n/aop/images/medium/ja-2011-08647n_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja208647n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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3D Proteins: Getting the Big Picture - Drug Discovery & Development
3D Proteins: Getting the Big Picture - Drug Discovery & Development
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Drug Discovery & Development
<img alt="" height="1" width="1" />
3D Proteins: Getting the Big Picture
Drug Discovery & Development
For decades, with funding from the National Science Foundation (NSF), Hinton has used nuclear magnetic resonance (NMR) to look at protein structure and function. But he wanted to find a way to educate and engage students about his discoveries. ...
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05-10-2011 07:17 PM
[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
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[NMR paper] High pressure NMR study of a small protein, gurmarin.
High pressure NMR study of a small protein, gurmarin.
Related Articles High pressure NMR study of a small protein, gurmarin.
J Biomol NMR. 1998 Nov;12(4):535-41
Authors: Inoue K, Yamada H, Imoto T, Akasaka K
The effect of pressure on the structure of gurmarin, a globular, 35-residue protein from Gymnema sylvestre, was studied in aqueous environment (95% 1H2O/5% 2H2O, pH 2.0) with an on-line variable pressure NMR system operating at 750 MHz. Two-dimensional TOCSY and NOESY spectra were measured as functions of pressure between 1 and 2000 bar at...
NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review.
Linear Mode
