[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 attach an amino acid to its cognate tRNA isoacceptors through an ester bond. The standard set of 20 amino acids implies 20 aaRSs for each pair of amino acid/tRNA isoacceptors. However, the genomes of all archaea and some bacteria do not encode for a complete set of 20 aaRSs. For the human pathogenic bacterium Helicobacter pylori, a gene encoding asparaginyl-tRNA synthetase (AsnRS) is absent whilst an aspartyl-tRNA synthetase (AspRS) aminoacylates both tRNAAsp and tRNAAsn with aspartate. The structural and functional basis for this non-discriminatory behavior is not well understood. Here we report the over-production of the N-terminal anticodon-binding domain of H. pylori ND-AspRS using Escherichia coli BL21(DE3) host cells. Prolonged expression of this protein resulted in a toxic phenotype, limiting the expression period to just 30 minutes. Purified protein was monomeric in solution by gel filtration chromatography and stable up to 42 oC as observed in temperature-dependent dynamic light scattering measurements. Circular dichroism indicated a mixture of ?-helix and ?-sheet secondary structure at 20 oC and predominantly ?-sheet at 70 oC. Optimized crystallization conditions at pH 5.6 with PEG 4000 as a co-precipitant produced well-formed crystals and 1H NMR spectrum shows a well dispersed chemical shift envelope characteristic of a folded protein.
PMID: 23454362 [PubMed - as supplied by publisher]
[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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NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi200189u/aop/images/medium/bi-2011-00189u_0010.gif
Biochemistry
DOI: 10.1021/bi200189u
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NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
Biochemistry. 2011 Mar 25;
Authors: Paukstelis PJ, Chari N, Lambowitz AM, Hoffman DW
The mitochondrial tyrosyl-tRNA synthetases (mt TyrRSs) of Pezizomycotina fungi are bifunctional proteins that aminoacylate mitochondrial tRNATyr and are structure-stabilizing splicing cofactors for group I introns. Studies with the Neurospora...
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03-29-2011 07:04 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] NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding
NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.
Related Articles NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.
Chembiochem. 2003 Sep 5;4(9):870-7
Authors: Dehner A, Furrer J, Richter K, Schuster I, Buchner J, Kessler H
Hsp90 is one of the most abundant chaperone proteins in the cytosol. In an ATP-dependent manner it plays an essential role in the folding and activation of a...
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11-24-2010 09:16 PM
[NMR paper] Expanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase
Expanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase Activity of a Bacterial Expression Host Scott Ross was helpful in conducting the 1D TOCSY NMR experiments and Pratip Bhattachary is thanked for assistance in other NMR experiments. We are grateful to Yves Mechulam for a sample of plasmid pBSM547W305F and to Hieronim Jakubowski of UMDNJ-New Jersey Medical School, Newark, New Jersey, for plasmid pGG3. K.L.K. thanks the U.S. Department of Defense for a National Defense Science and Engineering Graduate Fellowship. This work was supported by grants from the...
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11-18-2010 09:15 PM
[NMR paper] Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'
Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
Protein Sci. 1994 Jul;3(7):1020-30
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[NMR paper] Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'
Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
Protein Sci. 1994 Jul;3(7):1020-30
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Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Linear Mode
