Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference38 articles.
1. Molecular basis of multidrug transport by ABC transporters
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1. The noncanonical nucleotide binding site 1 of the bile salt export pump is optimized for proper function of the transporter;Cell Biology International;2024-02-08
2. Asymmetric conformations and lipid interactions shape the ATP-coupled cycle of a heterodimeric ABC transporter;Nature Communications;2023-11-08
3. Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein;eLife;2023-10-02
4. Time‐Resolved Mn2+−NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter**;Angewandte Chemie International Edition;2023-08-07
5. Zeitaufgelöste Mn2+−NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter**;Angewandte Chemie;2023-08-07
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