Related ArticlesComplexes of Escherichia coli adenylate kinase and nucleotides: 1H NMR studies of the nucleotide sites in solution.
Biochemistry. 1990 Aug 14;29(32):7459-67
Authors: Vetter IR, Reinstein J, Rösch P
One- and two-dimensional nuclear magnetic resonance (NMR) studies, in particular substrate--protein nuclear Overhauser effect (NOESY) measurements, as well as nucleotide and P1,P5-bis-(5'-adenosyl) pentaphosphate (AP5A) titrations and studies of the temperature-dependent unfolding of the tertiary structure of Escherichia coli adenylate kinase (AKEC) were performed. These experiments and comparison with the same type of experiments performed with the porcine enzyme [Rösch, P., Klaus, W., Auer, M., & Goody, R. S. (1989) Biochemistry 28, 4318-4325] led us to the following conclusions: (1) At pH 8 and concentrations of approximately 2.5-3 mM, AKEC is partially unfolded at 318 K. (2) ATP.Mg2+ binds to the ATP site with a dissociation constant of approximately 40 microM under the assumption that ATP binds to one nucleotide site only. (3) AP5A.Mg2+ binds to both nucleotide sites and thus simulates the active complex. (4) The ATP.Mg2+ adenine in the AKEC.AP5A.Mg2+ complex is located close to His134 and Phe19. (5) The AKEC "G-loop" with bound ATP.Mg2+ is structurally highly homologous to the loop region in the oncogene product p21 with bound GTP.Mg2+.
[NMR paper] A novel view of domain flexibility in E. coli adenylate kinase based on structural mo
A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
Related Articles A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
J Mol Biol. 2002 Jan 11;315(2):155-70
Authors: Tugarinov V, Shapiro YE, Liang Z, Freed JH, Meirovitch E
Adenylate kinase from Escherichia coli (AKeco), consisting of a single 23.6 kDa polypeptide chain folded into domains CORE, AMPbd and LID, catalyzes the reaction AMP+ATP-->2ADP. In the...
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[NMR paper] Escherichia coli diacylglycerol kinase: a case study in the application of solution N
Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
Biophys J. 1997 Jun;72(6):2688-701
Authors: Vinogradova O,...
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[NMR paper] Escherichia coli diacylglycerol kinase: a case study in the application of solution N
Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
Biophys J. 1997 Jun;72(6):2688-701
Authors: Vinogradova O,...
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[NMR paper] 13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with
13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with methotrexate and with folic acid.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with methotrexate and with folic acid.
FEBS Lett. 1992 Nov 9;312(2-3):147-51
Authors: Cheung HT, Birdsall B, Feeney J
13C NMR studies of 13C-labelled ligands bound to dihydrofolate reductase provide (DHFR) a powerful means of...
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[NMR paper] Studies on ribonucleoside-diphosphate reductase from Escherichia coli. The product dC
Studies on ribonucleoside-diphosphate reductase from Escherichia coli. The product dCDP is a competitive inhibitor and functions as a spectroscopic probe for the substrate binding site; demonstration by enzyme kinetics and 1H NMR.
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 Studies on ribonucleoside-diphosphate reductase from Escherichia coli. The product dCDP is a competitive inhibitor and functions as a spectroscopic probe for the substrate binding site;...
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[NMR paper] Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Related Articles Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Biochemistry. 1991 Apr 30;30(17):4137-42
Authors: Vetter IR, Konrad M, Rösch P
The role of one of the histidine residues present in many adenylate kinases (H36 in the porcine cytosolic enzyme) is highly disputed. We thus studied the yeast enzyme (AKye) containing this His residue. AKye is highly homologous to the Escherichia coli enzyme (AKec), a protein that is already well...
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[NMR paper] NMR studies of the activation of the Escherichia coli trp repressor.
NMR studies of the activation of the Escherichia coli trp repressor.
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 NMR studies of the activation of the Escherichia coli trp repressor.
Eur J Biochem. 1991 Nov 1;201(3):569-79
Authors: Hyde EI, Ramesh V, Frederick R, Roberts GC
The Escherichia coli trp repressor binds to the trp operator in the presence of tryptophan, thereby inhibiting tryptophan biosynthesis. Tryptophan analogues...
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[NMR paper] NMR studies of the activation of the Escherichia coli trp repressor.
NMR studies of the activation of the Escherichia coli trp repressor.
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 NMR studies of the activation of the Escherichia coli trp repressor.
Eur J Biochem. 1991 Nov 1;201(3):569-79
Authors: Hyde EI, Ramesh V, Frederick R, Roberts GC
The Escherichia coli trp repressor binds to the trp operator in the presence of tryptophan, thereby inhibiting tryptophan biosynthesis. Tryptophan analogues...