Structural and thermodynamic characterization of metal ion binding in Streptococcus suis Dpr.
Identifieur interne : 002429 ( Main/Exploration ); précédent : 002428; suivant : 002430Structural and thermodynamic characterization of metal ion binding in Streptococcus suis Dpr.
Auteurs : Teemu Haikarainen [Finlande] ; Angelos Thanassoulas ; Philemon Stavros ; George Nounesis ; Sauli Haataja ; Anastassios C. PapageorgiouSource :
- Journal of molecular biology [ 1089-8638 ] ; 2011.
Descripteurs français
- KwdFr :
- Calorimétrie, Conformation des protéines, Cristallographie aux rayons X, Céruloplasmine (), Céruloplasmine (métabolisme), Modèles chimiques, Métaux (), Métaux (métabolisme), Oxydoréduction, Protéines bactériennes (), Protéines bactériennes (métabolisme), Protéines de liaison à l'ADN (), Protéines de liaison à l'ADN (métabolisme), Sites de fixation, Streptococcus suis (enzymologie).
- MESH :
- enzymologie : Streptococcus suis.
- métabolisme : Céruloplasmine, Métaux, Protéines bactériennes, Protéines de liaison à l'ADN.
- Calorimétrie, Conformation des protéines, Cristallographie aux rayons X, Céruloplasmine, Modèles chimiques, Métaux, Oxydoréduction, Protéines bactériennes, Protéines de liaison à l'ADN, Sites de fixation.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Binding Sites, Calorimetry, Ceruloplasmin (chemistry), Ceruloplasmin (metabolism), Crystallography, X-Ray, DNA-Binding Proteins (chemistry), DNA-Binding Proteins (metabolism), Metals (chemistry), Metals (metabolism), Models, Chemical, Oxidation-Reduction, Protein Conformation, Streptococcus suis (enzymology).
- MESH :
- chemical , chemistry : Bacterial Proteins, Ceruloplasmin, DNA-Binding Proteins, Metals.
- chemical , metabolism : Bacterial Proteins, Ceruloplasmin, DNA-Binding Proteins, Metals.
- enzymology : Streptococcus suis.
- Binding Sites, Calorimetry, Crystallography, X-Ray, Models, Chemical, Oxidation-Reduction, Protein Conformation.
Abstract
The use of protein cages for the creation of novel inorganic nanomaterials has attracted considerable attention in recent years. Ferritins are among the most commonly used protein cages in nanoscience. Accordingly, the binding of various metals to ferritins has been studied extensively. Dps (DNA-binding protein from starved cells)-like proteins belong to the ferritin superfamily. In contrast to ferritins, Dps-like proteins form 12-mers instead of 24-mers, have a different ferroxidase center, and are able to store a smaller amount of iron atoms in a hollow cavity (up to ∼500, instead of the ∼4500 iron atoms found in ferritins). With the exception of iron, the binding of other metal cations to Dps proteins has not been studied in detail. Here, the binding of six divalent metal ions (Zn(2+), Mn(2+), Ni(2+), Co(2+), Cu(2+), and Mg(2+)) to Streptococcus suisDps-like peroxide resistance protein (SsDpr) was characterized by X-ray crystallography and isothermal titration calorimetry (ITC). All metal cations, except for Mg(2+), were found to bind to the ferroxidase center similarly to Fe(2+), with moderate affinity (binding constants between 0.1×10(5) M(-1) and 5×10(5) M(-1)). The stoichiometry of binding, as deduced by ITC data, suggested the presence of a dication ferroxidase site. No other metal binding sites were identified in the protein. The results presented here demonstrate the ability of SsDpr to bind various metals as substitutes for iron and will help in better understanding protein-metal interactions in the Dps family of proteins as potential metal nanocontainers.
DOI: 10.1016/j.jmb.2010.10.058
PubMed: 21056572
Affiliations:
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Papageorgiou</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="eISSN">1089-8638</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (metabolism)</term><term>Binding Sites</term><term>Calorimetry</term><term>Ceruloplasmin (chemistry)</term><term>Ceruloplasmin (metabolism)</term><term>Crystallography, X-Ray</term><term>DNA-Binding Proteins (chemistry)</term><term>DNA-Binding Proteins (metabolism)</term><term>Metals (chemistry)</term><term>Metals (metabolism)</term><term>Models, Chemical</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Streptococcus suis (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Calorimétrie</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Céruloplasmine ()</term><term>Céruloplasmine (métabolisme)</term><term>Modèles chimiques</term><term>Métaux ()</term><term>Métaux (métabolisme)</term><term>Oxydoréduction</term><term>Protéines bactériennes ()</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines de liaison à l'ADN ()</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Sites de fixation</term><term>Streptococcus suis (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Ceruloplasmin</term><term>DNA-Binding Proteins</term><term>Metals</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Ceruloplasmin</term><term>DNA-Binding Proteins</term><term>Metals</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Streptococcus suis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Streptococcus suis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Céruloplasmine</term><term>Métaux</term><term>Protéines bactériennes</term><term>Protéines de liaison à l'ADN</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Calorimetry</term><term>Crystallography, X-Ray</term><term>Models, Chemical</term><term>Oxidation-Reduction</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Calorimétrie</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Céruloplasmine</term><term>Modèles chimiques</term><term>Métaux</term><term>Oxydoréduction</term><term>Protéines bactériennes</term><term>Protéines de liaison à l'ADN</term><term>Sites de fixation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The use of protein cages for the creation of novel inorganic nanomaterials has attracted considerable attention in recent years. Ferritins are among the most commonly used protein cages in nanoscience. Accordingly, the binding of various metals to ferritins has been studied extensively. Dps (DNA-binding protein from starved cells)-like proteins belong to the ferritin superfamily. In contrast to ferritins, Dps-like proteins form 12-mers instead of 24-mers, have a different ferroxidase center, and are able to store a smaller amount of iron atoms in a hollow cavity (up to ∼500, instead of the ∼4500 iron atoms found in ferritins). With the exception of iron, the binding of other metal cations to Dps proteins has not been studied in detail. Here, the binding of six divalent metal ions (Zn(2+), Mn(2+), Ni(2+), Co(2+), Cu(2+), and Mg(2+)) to Streptococcus suisDps-like peroxide resistance protein (SsDpr) was characterized by X-ray crystallography and isothermal titration calorimetry (ITC). All metal cations, except for Mg(2+), were found to bind to the ferroxidase center similarly to Fe(2+), with moderate affinity (binding constants between 0.1×10(5) M(-1) and 5×10(5) M(-1)). The stoichiometry of binding, as deduced by ITC data, suggested the presence of a dication ferroxidase site. No other metal binding sites were identified in the protein. The results presented here demonstrate the ability of SsDpr to bind various metals as substitutes for iron and will help in better understanding protein-metal interactions in the Dps family of proteins as potential metal nanocontainers.</div></front></TEI><affiliations><list><country><li>Finlande</li></country><region><li>Finlande occidentale</li></region><settlement><li>Turku</li></settlement></list><tree><noCountry><name sortKey="Haataja, Sauli" sort="Haataja, Sauli" uniqKey="Haataja S" first="Sauli" last="Haataja">Sauli Haataja</name><name sortKey="Nounesis, George" sort="Nounesis, George" uniqKey="Nounesis G" first="George" last="Nounesis">George Nounesis</name><name sortKey="Papageorgiou, Anastassios C" sort="Papageorgiou, Anastassios C" uniqKey="Papageorgiou A" first="Anastassios C" last="Papageorgiou">Anastassios C. Papageorgiou</name><name sortKey="Stavros, Philemon" sort="Stavros, Philemon" uniqKey="Stavros P" first="Philemon" last="Stavros">Philemon Stavros</name><name sortKey="Thanassoulas, Angelos" sort="Thanassoulas, Angelos" uniqKey="Thanassoulas A" first="Angelos" last="Thanassoulas">Angelos Thanassoulas</name></noCountry><country name="Finlande"><region name="Finlande occidentale"><name sortKey="Haikarainen, Teemu" sort="Haikarainen, Teemu" uniqKey="Haikarainen T" first="Teemu" last="Haikarainen">Teemu Haikarainen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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