Related ArticlesNMR Characterization of the Interaction of the Endonuclease Domain of MutL with Divalent Metal Ions and ATP.
PLoS One. 2014;9(6):e98554
Authors: Mizushima R, Kim JY, Suetake I, Tanaka H, Takai T, Kamiya N, Takano Y, Mishima Y, Tajima S, Goto Y, Fukui K, Lee YH
Abstract
MutL is a multi-domain protein comprising an N-terminal ATPase domain (NTD) and C-terminal dimerization domain (CTD), connected with flexible linker regions, that plays a key role in DNA mismatch repair. To expand understanding of the regulation mechanism underlying MutL endonuclease activity, our NMR-based study investigated interactions between the CTD of MutL, derived from the hyperthermophilic bacterium Aquifex aeolicus (aqMutL-CTD), and putative binding molecules. Chemical shift perturbation analysis with the model structure of aqMutL-CTD and circular dichroism results revealed that tight Zn2+ binding increased thermal stability without changing secondary structures to function at high temperatures. Peak intensity analysis exploiting the paramagnetic relaxation enhancement effect indicated the binding site for Mn2+, which shared binding sites for Zn2+. The coexistence of these two metal ions appears to be important for the function of MutL. Chemical shift perturbation analysis revealed a novel ATP binding site in aqMutL-CTD. A docking simulation incorporating the chemical shift perturbation data provided a putative scheme for the intermolecular interactions between aqMutL-CTD and ATP. We proposed a simple and understandable mechanical model for the regulation of MutL endonuclease activity in MMR based on the relative concentrations of ATP and CTD through ATP binding-regulated interdomain interactions between CTD and NTD.
PMID: 24901533 [PubMed - as supplied by publisher]
NMR Localization of Divalent Cations at the ActiveSite of the Neurospora VS Ribozyme Provides Insightsinto RNA–Metal-Ion Interactions
NMR Localization of Divalent Cations at the ActiveSite of the Neurospora VS Ribozyme Provides Insightsinto RNA–Metal-Ion Interactions
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi401484a/aop/images/medium/bi-2013-01484a_0009.gif
Biochemistry
DOI: 10.1021/bi401484a
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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nmrlearner
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01-11-2014 06:45 AM
NMR studies of alkali metal ions in organic and biological solids
NMR studies of alkali metal ions in organic and biological solids
February 2012
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 61</br>
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Highlights
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12-15-2012 09:51 AM
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 215</br>
Claudio Luchinat, Malini Nagulapalli, Giacomo Parigi, Luca Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively placed...
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03-09-2012 09:16 AM
NMR studies of alkali metal ions in organic and biological solids
NMR studies of alkali metal ions in organic and biological solids
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 61</br>
Gang Wu, Jianfeng Zhu</br>
</br>
</br></br>
nmrlearner
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03-09-2012 09:16 AM
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 30 December 2011</br>
Claudio*Luchinat, Malini*Nagulapalli, Giacomo*Parigi, Luca*Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively...
nmrlearner
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12-31-2011 10:40 AM
[NMR paper] NMR characterization of the interaction between the C-terminal domain of interferon-g
NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides.
Related Articles NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides.
Biochem J. 2004 Nov 15;384(Pt 1):93-9
Authors: Vanhaverbeke C, Simorre JP, Sadir R, Gans P, Lortat-Jacob H
Interferons are cytokines that play a complex role in the resistance of mammalian hosts to pathogens. IFNgamma (interferon-gamma) is secreted by activated T-cells and...
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11-24-2010 10:03 PM
[NMR paper] NMR spectroscopic studies of I = 1/2 metal ions in biological systems.
NMR spectroscopic studies of I = 1/2 metal ions in biological systems.
Related Articles NMR spectroscopic studies of I = 1/2 metal ions in biological systems.
Biochem Cell Biol. 1998;76(2-3):223-34
Authors: Oz G, Pountney DL, Armitage IM
This article reviews the use of nuclear magnetic resonance methods of spin 1/2 metal nuclei to probe the metal binding site(s) in a variety of metalloproteins. The majority of the studies have involved native Zn(II) and Ca(II) metalloproteins where there has been isostructural substitution of these metal ions...
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11-17-2010 11:06 PM
[NMR paper] Structural characterization of the divalent cation sites of bacterial phosphotriester
Structural characterization of the divalent cation sites of bacterial phosphotriesterase by 113Cd NMR spectroscopy.
Related Articles Structural characterization of the divalent cation sites of bacterial phosphotriesterase by 113Cd NMR spectroscopy.
Biochemistry. 1993 Sep 7;32(35):9148-55
Authors: Omburo GA, Mullins LS, Raushel FM
The phosphotriesterase from Pseudomonas diminuta catalyzes the hydrolysis of organophosphate esters. The isolated native protein contains zinc, and removal of this metal abolishes the enzymatic activity....