Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.
Identifieur interne : 003809 ( Main/Exploration ); précédent : 003808; suivant : 003810Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.
Auteurs : P. Jekow [Allemagne] ; J. Behlke ; W. Tichelaar ; R. Lurz ; M. Regalla ; W. Hinrichs ; P. TavaresSource :
- European journal of biochemistry [ 0014-2956 ] ; 1999.
Descripteurs français
- KwdFr :
- Cations divalents, Centrifugation en gradient de densité, Concentration osmolaire, Conformation des protéines, Glutaraldéhyde, Masse moléculaire, Microscopie électronique, Phages de Bacillus (), Phages de Bacillus (génétique), Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (isolement et purification), Protéines virales (), Protéines virales (génétique), Protéines virales (isolement et purification), Réactifs réticulants, Solutions, Stabilité de médicament.
- MESH :
- génétique : Phages de Bacillus, Protéines recombinantes, Protéines virales.
- isolement et purification : Protéines recombinantes, Protéines virales.
- Cations divalents, Centrifugation en gradient de densité, Concentration osmolaire, Conformation des protéines, Glutaraldéhyde, Masse moléculaire, Microscopie électronique, Phages de Bacillus, Protéines recombinantes, Protéines virales, Réactifs réticulants, Solutions, Stabilité de médicament.
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
Affiliations:
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Le document en format XML
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Tichelaar</name></author><author><name sortKey="Lurz, R" sort="Lurz, R" uniqKey="Lurz R" first="R" last="Lurz">R. Lurz</name></author><author><name sortKey="Regalla, M" sort="Regalla, M" uniqKey="Regalla M" first="M" last="Regalla">M. Regalla</name></author><author><name sortKey="Hinrichs, W" sort="Hinrichs, W" uniqKey="Hinrichs W" first="W" last="Hinrichs">W. Hinrichs</name></author><author><name sortKey="Tavares, P" sort="Tavares, P" uniqKey="Tavares P" first="P" last="Tavares">P. 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Jekow</name><affiliation wicri:level="3"><nlm:affiliation>Max Planck Institut für Molekulare Genetik, Berlin, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Max Planck Institut für Molekulare Genetik, Berlin</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation></author><author><name sortKey="Behlke, J" sort="Behlke, J" uniqKey="Behlke J" first="J" last="Behlke">J. Behlke</name></author><author><name sortKey="Tichelaar, W" sort="Tichelaar, W" uniqKey="Tichelaar W" first="W" last="Tichelaar">W. Tichelaar</name></author><author><name sortKey="Lurz, R" sort="Lurz, R" uniqKey="Lurz R" first="R" last="Lurz">R. Lurz</name></author><author><name sortKey="Regalla, M" sort="Regalla, M" uniqKey="Regalla M" first="M" last="Regalla">M. Regalla</name></author><author><name sortKey="Hinrichs, W" sort="Hinrichs, W" uniqKey="Hinrichs W" first="W" last="Hinrichs">W. Hinrichs</name></author><author><name sortKey="Tavares, P" sort="Tavares, P" uniqKey="Tavares P" first="P" last="Tavares">P. Tavares</name></author></analytic><series><title level="j">European journal of biochemistry</title><idno type="ISSN">0014-2956</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacillus Phages (chemistry)</term><term>Bacillus Phages (genetics)</term><term>Cations, Divalent</term><term>Centrifugation, Density Gradient</term><term>Cross-Linking Reagents</term><term>Drug Stability</term><term>Glutaral</term><term>Microscopy, Electron</term><term>Molecular Weight</term><term>Osmolar Concentration</term><term>Protein Conformation</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (isolation & purification)</term><term>Solutions</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (isolation & purification)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cations divalents</term><term>Centrifugation en gradient de densité</term><term>Concentration osmolaire</term><term>Conformation des protéines</term><term>Glutaraldéhyde</term><term>Masse moléculaire</term><term>Microscopie électronique</term><term>Phages de Bacillus ()</term><term>Phages de Bacillus (génétique)</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (isolement et purification)</term><term>Protéines virales ()</term><term>Protéines virales (génétique)</term><term>Protéines virales (isolement et purification)</term><term>Réactifs réticulants</term><term>Solutions</term><term>Stabilité de médicament</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Recombinant Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Recombinant Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cations, Divalent</term><term>Cross-Linking Reagents</term><term>Glutaral</term><term>Solutions</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bacillus Phages</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Bacillus Phages</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phages de Bacillus</term><term>Protéines recombinantes</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines recombinantes</term><term>Protéines virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Centrifugation, Density Gradient</term><term>Drug Stability</term><term>Microscopy, Electron</term><term>Molecular Weight</term><term>Osmolar Concentration</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cations divalents</term><term>Centrifugation en gradient de densité</term><term>Concentration osmolaire</term><term>Conformation des protéines</term><term>Glutaraldéhyde</term><term>Masse moléculaire</term><term>Microscopie électronique</term><term>Phages de Bacillus</term><term>Protéines recombinantes</term><term>Protéines virales</term><term>Réactifs réticulants</term><term>Solutions</term><term>Stabilité de médicament</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>Berlin</li></region><settlement><li>Berlin</li></settlement></list><tree><noCountry><name sortKey="Behlke, J" sort="Behlke, J" uniqKey="Behlke J" first="J" last="Behlke">J. Behlke</name><name sortKey="Hinrichs, W" sort="Hinrichs, W" uniqKey="Hinrichs W" first="W" last="Hinrichs">W. Hinrichs</name><name sortKey="Lurz, R" sort="Lurz, R" uniqKey="Lurz R" first="R" last="Lurz">R. Lurz</name><name sortKey="Regalla, M" sort="Regalla, M" uniqKey="Regalla M" first="M" last="Regalla">M. Regalla</name><name sortKey="Tavares, P" sort="Tavares, P" uniqKey="Tavares P" first="P" last="Tavares">P. Tavares</name><name sortKey="Tichelaar, W" sort="Tichelaar, W" uniqKey="Tichelaar W" first="W" last="Tichelaar">W. Tichelaar</name></noCountry><country name="Allemagne"><region name="Berlin"><name sortKey="Jekow, P" sort="Jekow, P" uniqKey="Jekow P" first="P" last="Jekow">P. Jekow</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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