Related ArticlesHigh pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase.
Biochemistry. 2000 Oct 24;39(42):12789-95
Authors: Kitahara R, Sareth S, Yamada H, Ohmae E, Gekko K, Akasaka K
A high-pressure (15)N/(1)H two-dimensional NMR study has been carried out on folate-bound dihydrofolate reductase (DHFR) from Escherichia coli in the pressure range between 30 and 2000 bar. Several cross-peaks in the (15)N/(1)H HSQC spectrum are split into two with increasing pressure, showing the presence of a second conformer in equilibrium with the first. Thermodynamic analysis of the pressure and temperature dependencies indicates that the second conformer is characterized by a smaller partial molar volume (DeltaV = -25 mL/mol at 15 degrees C) and smaller enthalpy and entropy values, suggesting that the second conformer is more open and hydrated than the first. The splittings of the cross-peaks (by approximately 1 ppm on (15)N axis at 2000 bar) arise from the hinges of the M20 loop, the C-helix, and the F-helix, all of which constitute the major binding site for the cofactor NADPH, suggesting that major differences in conformation occur in the orientations of the NADPH binding units. The Gibbs free energy of the second, open conformer is 5.2 kJ/mol above that of the first at 1 bar, giving an equilibrium population of about 10%. The second, open conformer is considered to be crucial for NADPH binding, and the NMR line width indicates that the upper limit for the rate of opening is 20 s(-)(1) at 2000 bar. These experiments show that high pressure NMR is a generally useful tool for detecting and analyzing "open" structures of a protein that may be directly involved in function.
Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR
Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR
Stepan B. Lesnichin, Ilya G. Shenderovich, Titin Muljati, David Silverman and Hans-Heinrich Limbach
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203478j/aop/images/medium/ja-2011-03478j_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203478j
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/pgOKoZytT3U
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[NMR paper] High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in
High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division.
Related Articles High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division.
J Mol Biol. 2000 Nov 24;304(2):219-29
Authors: Katoh E, Hatta T, Shindo H, Ishii Y, Yamada H, Mizuno T, Yamazaki T
YhhP, a small protein of 81 amino acid residues encoded by the yhhP gene in the Escherichia coli database, is implicated in cell division although the precise biological function of this protein has not been yet...
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11-19-2010 08:29 PM
[NMR paper] Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier
Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier transform infrared and NMR spectroscopy.
Related Articles Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier transform infrared and NMR spectroscopy.
Biochemistry. 1998 Dec 22;37(51):18001-9
Authors: Yamasaki K, Taniguchi Y, Takeda N, Nakano K, Yamasaki T, Kanaya S, Oobatake M
Pressure denaturation of Escherichia coli ribonuclease HI (RNase HI) was studied by Fourier transform infrared (FTIR) and two-dimensional 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] 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] Proton-transfer effects in the active-site region of Escherichia coli thioredoxin usi
Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
Related Articles Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
Biochemistry. 1991 Apr 30;30(17):4262-8
Authors: Dyson HJ, Tennant LL, Holmgren A
A series of two-dimensional (2D) correlated 1H NMR spectra of reduced and oxidized Escherichia coli thioredoxin have been used to probe the effects of pH in the vicinity of the active site, -Cys32-Gly-Pro-Cys35-, using the...