Related Articles19F 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 induces a conformational change, which enables the receptor to dock to the membrane components. To investigate the ligand-induced conformational change and binding properties of this protein, we used (19)F NMR to probe the four tryptophan residues located in the two lobes of the protein. The four tryptophan residues were labeled with 5-fluorotryptophan and assigned by site-directed mutagenesis. The (19)F NMR spectra of the partially ligand free proteins show broadened peaks which sharpen when L-leucine is bound, showing that the labeled wild-type protein and mutants are functional. The titration of L-phenylalanine into the 5-fluorotryptophan labeled wild-type protein shows the presence of closed and open conformers. Urea-induced denaturation studies support the NMR results that the wild-type protein binds L-phenylalanine in a different manner to L-leucine. Our studies showed that the tryptophan to phenylalanine mutations on structural units linked to the binding pocket produce subtle changes in the environment of Trp18 located directly in the binding cleft.
[NMR paper] Identification of the DNA binding surface of H-NS protein from Escherichia coli by he
Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
Related Articles Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
FEBS Lett. 1999 Jul 16;455(1-2):63-9
Authors: Shindo H, Ohnuki A, Ginba H, Katoh E, Ueguchi C, Mizuno T, Yamazaki T
The DNA binding domain of H-NS protein was studied with various N-terminal deletion mutant proteins and identified by gel retardation assay and heteronuclear 2D- and 3D-NMR...
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[NMR paper] Structural features of the binding site for ribosomal protein S8 in Escherichia coli
Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2139-44
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[NMR paper] Structural features of the binding site for ribosomal protein S8 in Escherichia coli
Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2139-44
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[NMR paper] Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its c
Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its complex with oligo DNAs.
Related Articles Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its complex with oligo DNAs.
Biol Pharm Bull. 1993 May;16(5):437-43
Authors: Shindo H, Kurumizaka H, Furubayashi A, Sakuma C, Matsumoto U, Yanagida A, Goshima N, Kano Y, Imamoto F
It was confirmed that the flexible arm region of HU alpha forms an antiparallel beta-sheet and that all of the residues of phenylalanines, together with some of...
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[NMR paper] Sequence-specific NMR assignments of the trp repressor from Escherichia coli using th
Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
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 Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
Eur J Biochem. 1992 Feb 15;204(1):137-46
Authors: Borden KL, Bauer CJ, Frenkiel TA, Beckmann P, Lane AN
...
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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...
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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...
19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesi
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