Related ArticlesNMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.
J Biol Chem. 2004 Aug 6;279(32):33958-67
Authors: Revington M, Holder TM, Zuiderweg ER
We present an NMR investigation of the nucleotide-dependent conformational properties of a 44-kDa nucleotide binding domain (NBD) of an Hsp70 protein. Conformational changes driven by ATP binding and hydrolysis in the N-terminal NBD are believed to allosterically regulate substrate affinity in the C-terminal substrate binding domain. Several crystal structures of Hsc70 NBDs in different nucleotide states have, however, not shown significant structural differences. We have previously reported the NMR assignments of the backbone resonances of the NBD of the bacterial Hsp70 homologue Thermus thermophilus DnaK in the ADP-bound state. In this study we show, by assigning the NBD with the ATP/transition state analogue, ADP.AlFx, bound, that it closely mimics the ATP-bound state. Chemical shift difference mapping of the two nucleotide states identified differences in a cluster of residues at the interface between subdomains 1A and 1B. Further analysis of the spectra revealed that the ATP state exhibited a single conformation, whereas the ADP state was in slow conformational exchange between a form similar to the ATP state and another state unique to the ADP-bound form. A model is proposed of the allosteric mechanism based on the nucleotide state altering the balance of a dynamic equilibrium between the open and closed states. The observed chemical shift perturbations were concentrated in an area close to a previously described J-domain binding channel, confirming the importance of that region in the allosteric mechanism.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Biochem Biophys Res Commun. 2010 Dec 24;
Authors: Myint W, Gong Q, Ahn J, Ishima R
Sarcoplasmic reticulum Ca(2+) ATPase (SERCA) is essential for muscle function by transporting Ca(2+) from the cytosol into the sarcoplasmic reticulum through ATP hydrolysis. In this report, the effects of substitution mutations on the...
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[NMR paper] Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of mu
Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.
Related Articles Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.
Biochem J. 2003 Dec 15;376(Pt 3):749-56
Authors: Ramaen O, Masscheleyn S, Duffieux F, Pamlard O, Oberkampf M, Lallemand JY, Stoven V, Jacquet E
Multidrug-resistance-associated...
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[NMR paper] Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubu
Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin studied by fluorescence and NMR spectroscopic methods.
Related Articles Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin studied by fluorescence and NMR spectroscopic methods.
Physiol Chem Phys Med NMR. 2001;33(2):139-51
Authors: Kuchroo K, Maity H, Kasturi SR
Tubulin, the major protein of microtubules, has been shown to be an example of protein undergoing multistep unfolding. Local unfolding and stepwise loss of a...
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[NMR paper] NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide
NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
Related Articles NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
Cell. 1998 Oct 16;95(2):269-77
Authors: Liu X, Wang H, Eberstadt M, Schnuchel A, Olejniczak ET, Meadows RP, Schkeryantz JM, Janowick DA, Harlan JE, Harris EA, Staunton DE, Fesik SW
Guanine nucleotide exchange factors for the Rho family of GTPases contain a Dbl homology (DH) domain responsible for catalysis and a...
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[NMR paper] Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP inte
Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP interactions with the Fe protein of Klebsiella pneumoniae.
Related Articles Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP interactions with the Fe protein of Klebsiella pneumoniae.
Biochem J. 1998 Sep 15;334 ( Pt 3):601-7
Authors: Miller RW, Eady RR, Gormal C, Fairhurst SA, Smith BE
Investigation of the interaction of MgADP- and MgATP2- with the Fe protein of Klebsiella pneumoniae nitrogenase by 31P NMR showed that the adenine...
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[NMR paper] Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as mo
Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
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 Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
Eur J Biochem. 1993 Apr 15;213(2):781-8
Authors: Löw A, Sprinzl M, Limmer S
Proton-NMR signals in the downfield region (below approximately 10...
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[NMR paper] Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophil
Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR.
Related Articles Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR.
Biochemistry. 1992 Mar 24;31(11):2970-7
Authors: Limmer S, Reiser CO, Schirmer NK, Grillenbeck NW, Sprinzl M
Proton NMR experiments of the GTP/GDP-binding protein EF-Tu from the extremely thermophilic bacterium Thermus thermophilus HB8 in H2O have been performed paying special attention to the...
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[NMR paper] NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for
NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
Related Articles NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
Biochemistry. 1990 Apr 10;29(14):3509-14
Authors: Redfield AG, Papastavros MZ
The structure of the phosphoryl binding region of human N-ras p21 was probed by using heteronuclear proton-observed NMR methods. Normal protein and a Gly-12----Asp-12 mutant protein were prepared...
NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus t
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