Publikation:

On How the Conformational Cycle of the AcrB Efflux Pump is Coupled to Proton Translocation : a Theoretical Study Based on High-Resolution Structural Data

Lade...
Vorschaubild

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2011

Autor:innen

Anselmi, Claudio
Pos, Klaas M.
Faraldo-Gómez, José D.

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

URI (zitierfähiger Link)
ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Biophysical Journal. 2011, 100(3), pp. 412a. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2010.12.2442

Zusammenfassung

The AcrA/AcrB/TolC multidrug efflux pump confers Escherichia coli with antibiotic resistance by sequestering toxic compounds found within the periplasm and inner membrane and extruding them into the extracellular space. The AcrB trimer is the central component of this efflux complex; anchored in the inner membrane, it forms an asymmetric assembly that undergoes a conformational cycle in which each protomer adopts three different structures. As a result, substrates bound in the periplasmic domain of AcrB are projected into the TolC channel, which reaches beyond the outer membrane. Crucially, the conformational cycle within AcrB is driven by the translocation of protons down the gradient sustained by the inner membrane, through a mechanism that has not been characterized so far. Here, we investigate this microscopic mechanism through atomistic freeenergy molecular dynamics simulations and electrostatic calculations, based upon novel high-resolution structural data for wild-type and mutagenized AcrB. Specifically, we assess the events associated with binding and release of protons within the membrane domain, and determine the mechanism by which these events are coupled to the reorganization of key transmembrane helices within each protomer. This investigation reveals how proton translocation influences both local and remote interactions within the protein, thereby modulating its structure.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690ANSELMI, Claudio, Wenchang ZHOU, Kay DIEDERICHS, Klaas M. POS, José D. FARALDO-GÓMEZ, 2011. On How the Conformational Cycle of the AcrB Efflux Pump is Coupled to Proton Translocation : a Theoretical Study Based on High-Resolution Structural Data. In: Biophysical Journal. 2011, 100(3), pp. 412a. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2010.12.2442
BibTex
@article{Anselmi2011-02Confo-38196,
  year={2011},
  doi={10.1016/j.bpj.2010.12.2442},
  title={On How the Conformational Cycle of the AcrB Efflux Pump is Coupled to Proton Translocation : a Theoretical Study Based on High-Resolution Structural Data},
  number={3},
  volume={100},
  issn={0006-3495},
  journal={Biophysical Journal},
  author={Anselmi, Claudio and Zhou, Wenchang and Diederichs, Kay and Pos, Klaas M. and Faraldo-Gómez, José D.}
}
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/123456789/38196">
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-03-29T09:27:19Z</dcterms:available>
    <dc:contributor>Zhou, Wenchang</dc:contributor>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38196"/>
    <dc:creator>Faraldo-Gómez, José D.</dc:creator>
    <dc:contributor>Anselmi, Claudio</dc:contributor>
    <dc:contributor>Pos, Klaas M.</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Diederichs, Kay</dc:contributor>
    <dc:creator>Pos, Klaas M.</dc:creator>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-03-29T09:27:19Z</dc:date>
    <dc:creator>Diederichs, Kay</dc:creator>
    <dc:creator>Anselmi, Claudio</dc:creator>
    <dcterms:abstract>The AcrA/AcrB/TolC multidrug efflux pump confers Escherichia coli with antibiotic&#xD;
resistance by sequestering toxic compounds found within the periplasm&#xD;
and inner membrane and extruding them into the extracellular space. The AcrB&#xD;
trimer is the central component of this efflux complex; anchored in the inner&#xD;
membrane, it forms an asymmetric assembly that undergoes a conformational&#xD;
cycle in which each protomer adopts three different structures. As a result, substrates&#xD;
bound in the periplasmic domain of AcrB are projected into the TolC&#xD;
channel, which reaches beyond the outer membrane. Crucially, the conformational&#xD;
cycle within AcrB is driven by the translocation of protons down the gradient&#xD;
sustained by the inner membrane, through a mechanism that has not been&#xD;
characterized so far.&#xD;
Here, we investigate this microscopic mechanism through atomistic freeenergy&#xD;
molecular dynamics simulations and electrostatic calculations, based&#xD;
upon novel high-resolution structural data for wild-type and mutagenized&#xD;
AcrB. Specifically, we assess the events associated with binding and release&#xD;
of protons within the membrane domain, and determine the mechanism by&#xD;
which these events are coupled to the reorganization of key transmembrane helices&#xD;
within each protomer. This investigation reveals how proton translocation&#xD;
influences both local and remote interactions within the protein, thereby modulating&#xD;
its structure.</dcterms:abstract>
    <dc:creator>Zhou, Wenchang</dc:creator>
    <dc:contributor>Faraldo-Gómez, José D.</dc:contributor>
    <dc:language>eng</dc:language>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:title>On How the Conformational Cycle of the AcrB Efflux Pump is Coupled to Proton Translocation : a Theoretical Study Based on High-Resolution Structural Data</dcterms:title>
    <dcterms:issued>2011-02</dcterms:issued>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
  </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
Ja
Begutachtet
Diese Publikation teilen