ArticleThe Journal of biological chemistry2013
Hydrolysis at one of the two nucleotide-binding sites drives the dissociation of ATP-binding cassette nucleotide-binding domain dimers.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Genome-wide identification analysis of the ATP-binding cassette transporter family and expression analysis under methyl jasmonate treatment in Panax ginseng.BMC plant biology · 2025Article
- Conformational equilibrium of an ABC transporter analyzed by luminescence resonance energy transfer.Biophysical journal · 2025Article
- Interaction of a Homologous Series of Amphiphiles with P-glycoprotein in a Membrane Environment-Contributions of Polar and Non-Polar Interactions.Pharmaceutics · 2023Article
- Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA.Journal of the American Chemical Society · 2022Article
- Mapping Free Energy Pathways for ATP Hydrolysis in theMolecules (Basel, Switzerland) · 2018Article
- Persistence of the ABCC6 genes and the emergence of the bony skeleton in vertebrates.Scientific reports · 2018Article
- Comparison of mechanistic transport cycle models of ABC exporters.Biochimica et biophysica acta. Biomembranes · 2018Review
- Substrate-induced conformational changes in the nucleotide-binding domains of lipid bilayer-associated P-glycoprotein during ATP hydrolysis.The Journal of biological chemistry · 2017Article
- The Lipid Bilayer Modulates the Structure and Function of an ATP-binding Cassette Exporter.The Journal of biological chemistry · 2016Article
- Toward Determining ATPase Mechanism in ABC Transporters: Development of the Reaction Path-Force Matching QM/MM Method.Methods in enzymology · 2016Article
- The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein.The Journal of biological chemistry · 2015Article
- In silico screening for inhibitors of p-glycoprotein that target the nucleotide binding domains.Molecular pharmacology · 2014Article
- ATP binding to two sites is necessary for dimerization of nucleotide-binding domains of ABC proteins.Biochemical and biophysical research communications · 2014Article
- Functional analysis and regulation of purified connexin hemichannels.Frontiers in physiology · 2014Review
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2 authors.
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Abstract
The functional unit of ATP-binding cassette (ABC) transporters consists of two transmembrane domains and two nucleotide-binding domains (NBDs). ATP binding elicits association of the two NBDs, forming a dimer in a head-to-tail arrangement, with two nucleotides "sandwiched" at the dimer interface. Each of the two nucleotide-binding sites is formed by residues from the two NBDs. We recently found that the prototypical NBD MJ0796 from Methanocaldococcus jannaschii dimerizes in response to ATP binding and dissociates completely following ATP hydrolysis. However, it is still unknown whether dissociation of NBD dimers follows ATP hydrolysis at one or both nucleotide-binding sites. Here, we used luminescence resonance energy transfer to study heterodimers formed by one active (donor-labeled) and one catalytically defective (acceptor-labeled) NBD. Rapid mixing experiments in a stop-flow chamber showed that NBD heterodimers with one functional and one inactive site dissociated at a rate indistinguishable from that of dimers with two hydrolysis-competent sites. Comparison of the rates of NBD dimer dissociation and ATP hydrolysis indicated that dissociation followed hydrolysis of one ATP. We conclude that ATP hydrolysis at one nucleotide-binding site drives NBD dimer dissociation.
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