@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.}
}

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    <dc:contributor>Zhou, Wenchang</dc:contributor>
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    <dc:creator>Faraldo-Gómez, José D.</dc:creator>
    <dc:contributor>Anselmi, Claudio</dc:contributor>
    <dc:contributor>Pos, Klaas M.</dc:contributor>
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    <dc:contributor>Diederichs, Kay</dc:contributor>
    <dc:creator>Pos, Klaas M.</dc:creator>
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    <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>
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    <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>
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