Publication: Split tasks of asymmetric nucleotide-binding sites in the heterodimeric ABC exporter EfrCD
Split tasks of asymmetric nucleotide-binding sites in the heterodimeric ABC exporter EfrCD
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Hürlimann, L. M., Hohl, M., & Seeger, M. A. (2017). Split tasks of asymmetric nucleotide-binding sites in the heterodimeric ABC exporter EfrCD. FEBS Journal, 284, 1672–1687. https://doi.org/10.1111/febs.14065
Abstract
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Abstract
Many heterodimeric ATP-binding cassette (ABC) exporters evolved asymmetric ATP-binding sites containing a degenerate site incapable of ATP hydrolysis due to noncanonical substitutions in conserved sequence motifs. Recent studies revealed that nucleotide binding to the degenerate site stabilizes contacts between the nucleotide-binding domains (NBDs) of the inward-facing transporter and regulates ATP hydrolysis at the consensus site via allosteric coupling mediated by the D-loops. However, it is unclear whether nucleotide binding to the
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- Hürlimann, Lea M
- Hohl, Michael
- Seeger, Markus A
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Hürlimann, L. M., Hohl, M., & Seeger, M. A. (2017). Split tasks of asymmetric nucleotide-binding sites in the heterodimeric ABC exporter EfrCD. FEBS Journal, 284, 1672–1687. https://doi.org/10.1111/febs.14065