Related ArticlesNMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Biochemistry. 1991 Nov 12;30(45):10872-7
Authors: Lowry DF, Cool RH, Redfield AG, Parmeggiani A
The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide groups of Lys 24 and Gly 83. These are conserved residues in each of the consensus sequences. Their uncharacteristic downfield proton shifts are attributed to strong hydrogen bonds to phosphate oxygens as for resonances in N-ras-p21 [Redfield, A. G., & Papastavros, M. Z. (1990) Biochemistry 29, 3509-3514]. The Lys 24 of the EF-Tu G-domain has nearly the same proton and nitrogen shifts as the corresponding Lys 16 in p21. These results suggest that this conserved lysine has a similar structural role in proteins in this class. The tentative Gly 83 resonance has no spectral analogue in p21. A mutant protein with His 84 changed to glycine was fully 15N-labeled and the proton resonance assigned to Gly 83 shifted downfield by 0.3 ppm, thereby supporting the assignment.
[NMR paper] 19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesi
19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesis and assignment of the 5-fluorotryptophan-labeled residues.
Related Articles 19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesis and assignment of the 5-fluorotryptophan-labeled residues.
Protein Eng. 2002 Nov;15(11):855-9
Authors: Salopek-Sondi B, Luck LA
The Escherichia coli L-leucine receptor is an aqueous protein and the first component in the distinct transport pathway for hydrophobic amino acids. L-leucine binding...
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[NMR paper] The NMR structure of the RNA binding domain of E. coli rho factor suggests possible R
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Related Articles The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Nat Struct Biol. 1998 May;5(5):393-9
Authors: Briercheck DM, Wood TC, Allison TJ, Richardson JP, Rule GS
Rho protein is an essential hexameric RNA-DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding...
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[NMR paper] The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli pho
The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.
FEBS Lett. 1993 Jan 2;315(1):11-5
Authors: van Nuland NA, Kroon GJ, Dijkstra K, Wolters GK, Scheek RM, Robillard GT
The region of the surface of...
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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] Examination of elongation factor Tu for aluminum fluoride binding sites using fluores
Examination of elongation factor Tu for aluminum fluoride binding sites using fluorescence and 19F-NMR methodologies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Examination of elongation factor Tu for aluminum fluoride binding sites using fluorescence and 19F-NMR methodologies.
FEBS Lett. 1991 Jan 28;278(2):225-8
Authors: Hazlett TL, Higashijima T, Jameson DM
This article reports on a comparison of the interaction of Al3+ and F- with two GTP-binding proteins,...
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[NMR paper] 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containin
1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
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Arch Biochem Biophys. 1991 Dec;291(2):307-10
Authors: Panth H, Brenner MC, Wu FY
The DNA-dependent RNA polymerase containing two intrinsic cobalt ions (Co2-RPase) instead of the naturally occurring zinc was purified from Escherichia coli cells grown in zinc-depleted, cobalt-enriched media....
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[NMR paper] 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containin
1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
Related Articles 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
Arch Biochem Biophys. 1991 Dec;291(2):307-10
Authors: Panth H, Brenner MC, Wu FY
The DNA-dependent RNA polymerase containing two intrinsic cobalt ions (Co2-RPase) instead of the naturally occurring zinc was purified from Escherichia coli cells grown in zinc-depleted, cobalt-enriched media....
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[NMR paper] NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu
NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Related Articles NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Biochemistry. 1991 Nov 12;30(45):10872-7
Authors: Lowry DF, Cool RH, Redfield AG, Parmeggiani A
The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide...
NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu
Linear Mode
