Ion transport and energy transduction of P-type ATPases studied by simulations

Lade...
Vorschaubild
Dateien
Zu diesem Dokument gibt es keine Dateien.
Datum
2009
Autor:innen
Siu, Shirley W. I.
Böckmann, Rainer A.
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
ArXiv-ID
Internationale Patentnummer
EU-Projektnummer
DFG-Projektnummer
Projekt
Open Access-Veröffentlichung
Sammlungen
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
unikn.publication.listelement.citation.prefix.version.undefined
European Biophysics Journal. 2009, 38(S1), pp. 35-212. ISSN 0175-7571. eISSN 1432-1017. Available under: doi: 10.1007/s00249-009-0478-1
Zusammenfassung

P-type ATPases actively transport cations across the membrane. The basic mechanisms of ion transport and energy transduction are supposed to be the same in all P-type ATPases. Both reaction mechanisms were studied computationally for the Ca2+-ATPase and Na+/K+-ATPase. The Ca2+ transport of the Ca2+-ATPase is associated with a proton countertransport from the SR to the cytoplasm. Binding of the protons is thought to take place at acidic residues in the binding sites. The protonation of acidic ligands were analyzed in different enzyme states of the Ca2+-ATPase by multiconformation continuum electrostatic calculations. Glu771, Asp800 and Glu908 are prime candidates for the proton countertransporting residues and are likely to receive and release their proton via the same path. The Glu309 instead might serve as a proton shuttle between Ca2+ binding site I and the cytoplasm. The reaction cycle of P-Type ATPases is physiologically initiated by the binding and hydrolysis of ATP but can also be induced experimentally by voltage jumps across the membrane. We simulated the applied electric field by an “ionic capacitor” and studied the impact on different enzyme states of the Ca2+-ATPase and the Na+/K+-ATPase by a combination of MCCE and MD. A selective activation of specific helices in response to the electric field is observed.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Konferenz
7th EBSA European Biophysics Congress, 11. Juli 2009 - 15. Juli 2009, Genova, Italy
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690WEIDEMÜLLER, Christian, Shirley W. I. SIU, Rainer A. BÖCKMANN, Karin HAUSER, 2009. Ion transport and energy transduction of P-type ATPases studied by simulations. 7th EBSA European Biophysics Congress. Genova, Italy, 11. Juli 2009 - 15. Juli 2009. In: European Biophysics Journal. 2009, 38(S1), pp. 35-212. ISSN 0175-7571. eISSN 1432-1017. Available under: doi: 10.1007/s00249-009-0478-1
BibTex
@article{Weidemuller2009-07trans-17529,
  year={2009},
  doi={10.1007/s00249-009-0478-1},
  title={Ion transport and energy transduction of P-type ATPases studied by simulations},
  number={S1},
  volume={38},
  issn={0175-7571},
  journal={European Biophysics Journal},
  pages={35--212},
  author={Weidemüller, Christian and Siu, Shirley W. I. and Böckmann, Rainer A. and Hauser, Karin}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/17529">
    <dc:contributor>Böckmann, Rainer A.</dc:contributor>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/17529"/>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:abstract xml:lang="eng">P-type ATPases actively transport cations across the membrane. The basic mechanisms of ion transport and energy transduction are supposed to be the same in all P-type ATPases. Both reaction mechanisms were studied computationally for the Ca2+-ATPase and Na+/K+-ATPase. The Ca2+ transport of the Ca2+-ATPase is associated with a proton countertransport from the SR to the cytoplasm. Binding of the protons is thought to take place at acidic residues in the binding sites. The protonation of acidic ligands were analyzed in different enzyme states of the Ca2+-ATPase by multiconformation continuum electrostatic calculations. Glu771, Asp800 and Glu908 are prime candidates for the proton countertransporting residues and are likely to receive and release their proton via the same path. The Glu309 instead might serve as a proton shuttle between Ca2+ binding site I and the cytoplasm. The reaction cycle of P-Type ATPases is physiologically initiated by the binding and hydrolysis of ATP but can also be induced experimentally by voltage jumps across the membrane. We simulated the applied electric field by an “ionic capacitor” and studied the impact on different enzyme states of the Ca2+-ATPase and the Na+/K+-ATPase by a combination of MCCE and MD. A selective activation of specific helices in response to the electric field is observed.</dcterms:abstract>
    <dc:contributor>Hauser, Karin</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-19T14:56:33Z</dc:date>
    <dcterms:title>Ion transport and energy transduction of P-type ATPases studied by simulations</dcterms:title>
    <dc:creator>Böckmann, Rainer A.</dc:creator>
    <dc:contributor>Siu, Shirley W. I.</dc:contributor>
    <dcterms:bibliographicCitation>Publ. in: European Biophysics Journal ; 38 (2009), Suppl. 1 "7th EBSA European Biophysics Congress, July 11-15 2009, Genova, Italy". - S. S59</dcterms:bibliographicCitation>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-19T14:56:33Z</dcterms:available>
    <dc:creator>Weidemüller, Christian</dc:creator>
    <dc:language>eng</dc:language>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:rights>terms-of-use</dc:rights>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Hauser, Karin</dc:creator>
    <dc:contributor>Weidemüller, Christian</dc:contributor>
    <dcterms:issued>2009-07</dcterms:issued>
    <dc:creator>Siu, Shirley W. I.</dc:creator>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet