Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.
Identifieur interne : 002620 ( PubMed/Corpus ); précédent : 002619; suivant : 002621Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.
Auteurs : P. Jekow ; J. Behlke ; W. Tichelaar ; R. Lurz ; M. Regalla ; W. Hinrichs ; P. TavaresSource :
- European journal of biochemistry [ 0014-2956 ] ; 1999.
English descriptors
- KwdEn :
- Bacillus Phages (chemistry), Bacillus Phages (genetics), Cations, Divalent, Centrifugation, Density Gradient, Cross-Linking Reagents, Drug Stability, Glutaral, Microscopy, Electron, Molecular Weight, Osmolar Concentration, Protein Conformation, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Solutions, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (isolation & purification).
- MESH :
- chemical , chemistry : Recombinant Proteins, Viral Proteins.
- chemical , genetics : Recombinant Proteins, Viral Proteins.
- chemical , isolation & purification : Recombinant Proteins, Viral Proteins.
- chemical : Cations, Divalent, Cross-Linking Reagents, Glutaral, Solutions.
- chemistry : Bacillus Phages.
- genetics : Bacillus Phages.
- Centrifugation, Density Gradient, Drug Stability, Microscopy, Electron, Molecular Weight, Osmolar Concentration, Protein Conformation.
Abstract
Bacteriophage SPP1 portal protein is a large cyclical homo-oligomer composed of 13 subunits. The solution structure and assembly behavior of this protein with high-point rotational symmetry was characterized. The purified protein was present as a monodisperse population of 13-mers, named gp6H, at univalent salt concentrations in the hundred millimolar range (>/= 250 mM NaCl) or in the presence of bivalent cations in the millimolar range (>/= 5 mM MgCl2). Gp6H had a slightly higher sedimentation coefficient, a smaller shape-dependent frictional ratio, and a higher rate of intersubunit cross-linking in the presence of magnesium than in its absence. In the absence of bivalent cations and at univalent salt concentrations below 250 mM, the 13-mer molecules dissociated partially into stable monomers, named gp6L. The monomer had a somewhat different shape from the subunit present in the 13-mer, but maintained a defined tertiary structure. The association-dissociation equilibrium was mainly between the monomer and the 13-mer with a minor population of intermediate oligomers. Their interconversion was strongly influenced by the ionic environment. Under physiological conditions, the concentration of Mg2+ found in the Bacillus subtilis cytoplasm (10-50 mM) probably promotes complete association of gp6 into 13-mer rings with a compact conformation.
DOI: 10.1046/j.1432-1327.1999.00601.x
PubMed: 10491118
Links to Exploration step
pubmed:10491118Le document en format XML
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<front><div type="abstract" xml:lang="en">Bacteriophage SPP1 portal protein is a large cyclical homo-oligomer composed of 13 subunits. The solution structure and assembly behavior of this protein with high-point rotational symmetry was characterized. The purified protein was present as a monodisperse population of 13-mers, named gp6H, at univalent salt concentrations in the hundred millimolar range (>/= 250 mM NaCl) or in the presence of bivalent cations in the millimolar range (>/= 5 mM MgCl2). Gp6H had a slightly higher sedimentation coefficient, a smaller shape-dependent frictional ratio, and a higher rate of intersubunit cross-linking in the presence of magnesium than in its absence. In the absence of bivalent cations and at univalent salt concentrations below 250 mM, the 13-mer molecules dissociated partially into stable monomers, named gp6L. The monomer had a somewhat different shape from the subunit present in the 13-mer, but maintained a defined tertiary structure. The association-dissociation equilibrium was mainly between the monomer and the 13-mer with a minor population of intermediate oligomers. Their interconversion was strongly influenced by the ionic environment. Under physiological conditions, the concentration of Mg2+ found in the Bacillus subtilis cytoplasm (10-50 mM) probably promotes complete association of gp6 into 13-mer rings with a compact conformation.</div>
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<Abstract><AbstractText>Bacteriophage SPP1 portal protein is a large cyclical homo-oligomer composed of 13 subunits. The solution structure and assembly behavior of this protein with high-point rotational symmetry was characterized. The purified protein was present as a monodisperse population of 13-mers, named gp6H, at univalent salt concentrations in the hundred millimolar range (>/= 250 mM NaCl) or in the presence of bivalent cations in the millimolar range (>/= 5 mM MgCl2). Gp6H had a slightly higher sedimentation coefficient, a smaller shape-dependent frictional ratio, and a higher rate of intersubunit cross-linking in the presence of magnesium than in its absence. In the absence of bivalent cations and at univalent salt concentrations below 250 mM, the 13-mer molecules dissociated partially into stable monomers, named gp6L. The monomer had a somewhat different shape from the subunit present in the 13-mer, but maintained a defined tertiary structure. The association-dissociation equilibrium was mainly between the monomer and the 13-mer with a minor population of intermediate oligomers. Their interconversion was strongly influenced by the ionic environment. Under physiological conditions, the concentration of Mg2+ found in the Bacillus subtilis cytoplasm (10-50 mM) probably promotes complete association of gp6 into 13-mer rings with a compact conformation.</AbstractText>
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