Related ArticlesHigh-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substrate for ricin, a cytotoxic plant protein.
Nucleic Acids Res. 1996 Feb 15;24(4):611-8
Authors: Orita M, Nishikawa F, Kohno T, Senda T, Mitsui Y, Yaeta E, Kazunari T, Nishikawa S
Ricin is a cytotoxic plant protein that inactivates ribosomes by hydrolyzing the N-glycosidic bond at position A4324 in eukaryotic 28S rRNA. Recent studies showed that a four-nucleotide loop, GAGA, can function as a minimum substrate for ricin (the first adenosine corresponds to the site of depurination). We previously clarified the solution structure of this loop by NMR spectroscopy [Orita et al. (1993) Nucleic Acids Res. 21, 5670-5678]. To elucidate further details of the structural basis for recognition of its substrate by ricin, we studied the properties of a synthetic dodecanucleotide, r1C2U3C4A5G6dA7G8A9U10G11A12G (6dA12mer), which forms an RNA hairpin structure with a GdAGA loop and in which the site of depurination is changed from adenosine to 2'-deoxyadenosine. The N-glycosidase activity against the GdAGA loop of the A-chain of ricin was 26 times higher than that against the GAGA loop. NMR studies indicated that the overall structure of the GdAGA loop was similar to that of the GAGA loop with the exception of the sugar puckers of 6dA and 7G. Therefore, it appears that the 2'-hydroxyl group of adenosine at the depurination site (6A) does not participate in the recognition by ricin of the substrate. Since the 2'-hydroxyl group can potentially destabilize the developing positive charge of the putative transition state intermediate, an oxycarbonium ion, the electronic effect may explain, at least in part, the faster rate of depurination of the GdAGA loop compared to that of GAGA loop. We also show that the amino group of 7G is essential for substrate recognition the ricin A-chain.
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using δ subunit (20 kDa) of Bacillus subtilis RNA polymerase...
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High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
Abstract Magic-angle spinning (MAS) solid-state NMR (SSNMR) spectroscopy of uniformly-13C,15N labeled protein samples provides insight into atomic-resolution chemistry and structure. Data collection efficiency has advanced remarkably in the last decade; however, the study of larger proteins is still challenged by relatively low resolution in comparison to solution NMR. In this study, we present a systematic analysis of SSNMR protein spectra acquired at 11.7, 17.6 and 21.1 Tesla (1H frequencies of...
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[NMR paper] A high-resolution NMR study of long-lived water molecules in both oxidation states of
A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
Related Articles A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
Biochemistry. 2003 Apr 1;42(12):3457-63
Authors: Bertini I, Ghosh K, Rosato A, Vasos PR
The interaction of water with oxidized and reduced cytochrome c from the Gram-positive bacterium Bacillus pasteurii (a 71-amino acid long monoheme cytochrome) is investigated through CLEANEX experiments and (15)N-edited...
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Improved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Exper
Improved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Experiment.
Related Articles Improved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Experiment.
Chem Phys Lett. 2010 Jul 9;494(1-3):104-110
Authors: Gopinath T, Veglia G
The atomic structure of small molecules and polypeptides can be attained from anisotropic NMR parameters such as dipolar couplings (DC) and chemical shifts (CS). Separated local field experiments resolve DC and CS correlations into two dimensions. However, crowded NMR...
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[NMR paper] High-resolution NMR study of a synthetic oligoribonucleotide with a tetranucleotide G
High-resolution NMR study of a synthetic oligoribonucleotide with a tetranucleotide GAGA loop that is a substrate for the cytotoxic protein, ricin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles High-resolution NMR study of a synthetic oligoribonucleotide with a tetranucleotide GAGA loop that is a substrate for the cytotoxic protein, ricin.
Nucleic Acids Res. 1993 Dec 11;21(24):5670-8
Authors: Orita M, Nishikawa F, Shimayama T, Taira K, Endo Y, Nishikawa S
...
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[NMR paper] A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c
A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex.
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 A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex.
Eur J Biochem. 1992 Sep 15;208(3):713-20
Authors: Tuzi S,...
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[NMR paper] High-resolution NMR study of the pressure-induced unfolding of lysozyme.
High-resolution NMR study of the pressure-induced unfolding of lysozyme.
Related Articles High-resolution NMR study of the pressure-induced unfolding of lysozyme.
Biochemistry. 1992 Sep 1;31(34):7773-8
Authors: Samarasinghe SD, Campbell DM, Jonas A, Jonas J
The pressure-induced reversible unfolding of lysozyme was investigated by high-resolution proton magnetic resonance spectroscopy by following the proton spectra of the following residues: His-15 epsilon 1, Trp-28 epsilon 3, Leu-17 delta 2, Cys-64 alpha, and Trp-108 epsilon 3. The...
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[NMR paper] High-resolution 13C NMR study of the topography and dynamics of methionine residues i
High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin.
Related Articles High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin.
Biochemistry. 1991 Apr 23;30(16):3885-92
Authors: Seigneuret M, Neumann JM, Levy D, Rigaud JL
The proton transport membrane protein bacteriorhodopsin has been biosynthetically labeled with methionine and studied by high-resolution 13C NMR after solubilization in the detergent...