Simulation of the Coupling between Nucleotide Binding and Transmembrane Domains in the ATP Binding Cassette Transporter BtuCD

Jacon Sonne, Chriatian Kandt, Günther H. Peters, Flemming Y. Hansen, Morten Østergaard Jensen, D. Peter Tieleman

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

    Resumé

    The nucleotide-induced structural rearrangements in ATP binding cassette (ABC) transporters, leading to substrate translocation, are largely unknown. We have modeled nucleotide binding and release in the vitamin B12 importer BtuCD using perturbed elastic network calculations and biased molecular dynamics simulations. Both models predict that nucleotide release decreases the tilt between the two transmembrane domains and opens the cytoplasmic gate. Nucleotide binding has the opposite effect. The observed coupling may be relevant for all ABC transporters because of the conservation of nucleotide binding domains and the shared role of ATP in ABC transporters. The rearrangements in the cytoplasmic gate region do not provide enough space for B12 to diffuse from the transporter pore into the cytoplasm, which could suggest that peristaltic forces are needed to exclude B12 from the transporter pore. Copyright © 2007 by the Biophysical Society.
    OriginalsprogEngelsk
    TidsskriftBiophysical Journal
    Vol/bind92
    Udgave nummer8
    Sider (fra-til)2727-2734
    Antal sider8
    ISSN0006-3495
    DOI
    StatusUdgivet - 2007

    Citer dette

    Sonne, Jacon ; Kandt, Chriatian ; Peters, Günther H. ; Hansen, Flemming Y. ; Jensen, Morten Østergaard ; Tieleman, D. Peter. / Simulation of the Coupling between Nucleotide Binding and Transmembrane Domains in the ATP Binding Cassette Transporter BtuCD. I: Biophysical Journal. 2007 ; Bind 92, Nr. 8. s. 2727-2734.
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    title = "Simulation of the Coupling between Nucleotide Binding and Transmembrane Domains in the ATP Binding Cassette Transporter BtuCD",
    abstract = "The nucleotide-induced structural rearrangements in ATP binding cassette (ABC) transporters, leading to substrate translocation, are largely unknown. We have modeled nucleotide binding and release in the vitamin B12 importer BtuCD using perturbed elastic network calculations and biased molecular dynamics simulations. Both models predict that nucleotide release decreases the tilt between the two transmembrane domains and opens the cytoplasmic gate. Nucleotide binding has the opposite effect. The observed coupling may be relevant for all ABC transporters because of the conservation of nucleotide binding domains and the shared role of ATP in ABC transporters. The rearrangements in the cytoplasmic gate region do not provide enough space for B12 to diffuse from the transporter pore into the cytoplasm, which could suggest that peristaltic forces are needed to exclude B12 from the transporter pore. Copyright {\circledC} 2007 by the Biophysical Society.",
    author = "Jacon Sonne and Chriatian Kandt and Peters, {G{\"u}nther H.} and Hansen, {Flemming Y.} and Jensen, {Morten {\O}stergaard} and Tieleman, {D. Peter}",
    year = "2007",
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    language = "English",
    volume = "92",
    pages = "2727--2734",
    journal = "Biophysical Journal",
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    Simulation of the Coupling between Nucleotide Binding and Transmembrane Domains in the ATP Binding Cassette Transporter BtuCD. / Sonne, Jacon; Kandt, Chriatian; Peters, Günther H.; Hansen, Flemming Y.; Jensen, Morten Østergaard; Tieleman, D. Peter.

    I: Biophysical Journal, Bind 92, Nr. 8, 2007, s. 2727-2734.

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

    TY - JOUR

    T1 - Simulation of the Coupling between Nucleotide Binding and Transmembrane Domains in the ATP Binding Cassette Transporter BtuCD

    AU - Sonne, Jacon

    AU - Kandt, Chriatian

    AU - Peters, Günther H.

    AU - Hansen, Flemming Y.

    AU - Jensen, Morten Østergaard

    AU - Tieleman, D. Peter

    PY - 2007

    Y1 - 2007

    N2 - The nucleotide-induced structural rearrangements in ATP binding cassette (ABC) transporters, leading to substrate translocation, are largely unknown. We have modeled nucleotide binding and release in the vitamin B12 importer BtuCD using perturbed elastic network calculations and biased molecular dynamics simulations. Both models predict that nucleotide release decreases the tilt between the two transmembrane domains and opens the cytoplasmic gate. Nucleotide binding has the opposite effect. The observed coupling may be relevant for all ABC transporters because of the conservation of nucleotide binding domains and the shared role of ATP in ABC transporters. The rearrangements in the cytoplasmic gate region do not provide enough space for B12 to diffuse from the transporter pore into the cytoplasm, which could suggest that peristaltic forces are needed to exclude B12 from the transporter pore. Copyright © 2007 by the Biophysical Society.

    AB - The nucleotide-induced structural rearrangements in ATP binding cassette (ABC) transporters, leading to substrate translocation, are largely unknown. We have modeled nucleotide binding and release in the vitamin B12 importer BtuCD using perturbed elastic network calculations and biased molecular dynamics simulations. Both models predict that nucleotide release decreases the tilt between the two transmembrane domains and opens the cytoplasmic gate. Nucleotide binding has the opposite effect. The observed coupling may be relevant for all ABC transporters because of the conservation of nucleotide binding domains and the shared role of ATP in ABC transporters. The rearrangements in the cytoplasmic gate region do not provide enough space for B12 to diffuse from the transporter pore into the cytoplasm, which could suggest that peristaltic forces are needed to exclude B12 from the transporter pore. Copyright © 2007 by the Biophysical Society.

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    DO - 10.1529/biophysj.106.097972

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    VL - 92

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    EP - 2734

    JO - Biophysical Journal

    JF - Biophysical Journal

    SN - 0006-3495

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    ER -