Related ArticlesCa2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy.
J Biol Chem. 1995 Sep 1;270(35):20643-52
Authors: Moser MJ, Lee SY, Klevit RE, Davis TN
As a first step toward identifying the important structural elements of calmodulin from Schizosaccharomyces pombe, we examined the ability of heterologous calmodulins and Ca(2+)-binding site mutant S. pombe calmodulins to replace the essential cam1+ gene. A cDNA encoding vertebrate calmodulin allows growth of S. pombe. However, calmodulin from Saccharomyces cerevisiae does not support growth even though the protein is produced at high levels. With one exception, all mutant S. pombe calmodulins with one or more intact Ca(2+)-binding sites allow growth at 21 degrees C. A mutant containing only an intact Ca(2+)-binding site 3 fails to support growth, as does S. pombe calmodulin with all four Ca(2+)-binding sites mutated. Several of the mutant proteins confer a temperature-sensitive phenotype. Analysis of the degree of temperature sensitivity allows the Ca(2+)-binding sites to be ranked by their ability to support fission yeast proliferation. Site 2 is more important than site 1, which is more important than site 4, which is more important than site 3. A visual colony color screen based on the fission yeast ade1+ gene was developed to perform these genetic analyses. To compare the Ca(2+)-binding properties of individual sites to their functional importance for viability, Ca2+ binding to calmodulin from S. pombe was studied by 1H NMR spectroscopy. NMR analysis indicates a Ca(2+)-binding profile that differs from those previously determined for vertebrate and S. cerevisiae calmodulins. Ca(2+)-binding site 3 has the highest relative affinity for Ca2+, while the affinities of sites 1, 2, and 4 are indistinguishable. A combination of an in vivo functional assay and an in vitro physical assay reveals that the relative affinity of a site for Ca2+ does not predict its functional importance.
[NMR software blog] Role Reversal
Role Reversal
In the beginning computers were computational tools with no graphic interface. From the user's point of view CW-NMR and FT-NMR were equivalent, because both of them plotted the results on paper and the analysis only began after printing. People ignored that FT spectrometers contained a computer and a program. Things changed with the structural determinations of biopolymers by Wüthrich and others. The 80s were a period of economical growth, protein NMR was a promising new field, Bill Gates was becoming the richest man in the world with his software company, so combining NMR...
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NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
J Biol Chem. 2011 Jul 28;
Authors: Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS
Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1) infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein...
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07-30-2011 11:23 AM
[NMR paper] Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-corre
Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements.
Related Articles Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements.
J Am Chem Soc. 2005 Jan 26;127(3):828-9
Authors: Wang T, Frederick KK, Igumenova TI, Wand AJ, Zuiderweg ER
The fast dynamics of protein backbones are often investigated by nuclear magnetic relaxation experiments that report on the degree of spatial restriction of the amide bond vector. By...
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11-24-2010 11:14 PM
[NMR paper] Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NM
Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.
Related Articles Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.
BMC Biochem. 2003 Dec 23;4:18
Authors: Fischer M, Schott AK, Kemter K, Feicht R, Richter G, Illarionov B, Eisenreich W, Gerhardt S, Cushman M, Steinbacher S, Huber R, Bacher A
BACKGROUND: Riboflavin synthase catalyzes the transformation of 6,7-dimethyl-8-ribityllumazine into riboflavin in...
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11-24-2010 09:16 PM
[NMR paper] CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in
CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
Related Articles CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
J Biol Chem. 2003 Dec 12;278(50):50175-81
Authors: Ziegler J, Sticht H, Marx UC, Müller W, Rösch P, Schwarzinger S
The conversion of prion helix 1 from an alpha-helical into an extended conformation is generally assumed to be an essential step in the conversion of the cellular isoform...
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11-24-2010 09:16 PM
[NMR paper] NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+
NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Related Articles NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Biochemistry. 1999 Sep 21;38(38):12320-32
Authors: Elshorst B, Hennig M, Försterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E
The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the...
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11-18-2010 08:31 PM
[NMR paper] Metal ion binding to calmodulin: NMR and fluorescence studies.
Metal ion binding to calmodulin: NMR and fluorescence studies.
Related Articles Metal ion binding to calmodulin: NMR and fluorescence studies.
Biometals. 1998 Sep;11(3):213-22
Authors: Ouyang H, Vogel HJ
Calmodulin is an important second messenger protein which is involved in a large variety of cellular pathways. Calmodulin is sensitive to fluctuations in the intracellular Ca2+ levels and is activated by the binding of four Ca2+ ions. In spite of the important role it plays in signal transduction pathways, it shows a surprisingly broad...
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11-17-2010 11:15 PM
[NMR paper] Triple-resonance multidimensional NMR study of calmodulin complexed with the binding
Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Related Articles Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Biochemistry. 1991 Jun 4;30(22):5498-504
Authors: Ikura M, Kay LE, Krinks M, Bax A
Heteronuclear 3D and 4D NMR experiments have been...
Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by m
Linear Mode
