ArticleThe Journal of biological chemistry2012
Kinetics of the association/dissociation cycle of an ATP-binding cassette nucleotide-binding domain.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Expression, Purification, and Structural Characterization of Membrane Proteins: A Case Study of the ABC Transporter MsbA.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Molecular Basis for the Activation ofJournal of the American Chemical Society · 2025Article
- Native mass spectrometry and structural studies reveal modulation of MsbA-nucleotide interactions by lipids.Nature communications · 2024Article
- Structural basis for lipid and copper regulation of the ABC transporter MsbA.Nature communications · 2022Article
- Conversion of chemical to mechanical energy by the nucleotide binding domains of ABCB1.Scientific reports · 2020Article
- Conformational rearrangements of the C1 ring in KaiC measure the timing of assembly with KaiB.Scientific reports · 2018Article
- 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
- Article
- ATP binding to two sites is necessary for dimerization of nucleotide-binding domains of ABC proteins.Biochemical and biophysical research communications · 2014Article
- Article
- Hydrolysis at one of the two nucleotide-binding sites drives the dissociation of ATP-binding cassette nucleotide-binding domain dimers.The Journal of biological chemistry · 2013Article
- Association/dissociation of the nucleotide-binding domains of the ATP-binding cassette protein MsbA measured during continuous hydrolysis.The Journal of biological chemistry · 2013Article
- Article
- A potentiator induces conformational changes on the recombinant CFTR nucleotide binding domains in solution.Cellular and molecular life sciences : CMLS · 2012Article
- Dissociation of ATP-binding cassette nucleotide-binding domain dimers into monomers during the hydrolysis cycle.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Most ATP binding cassette (ABC) proteins are pumps that transport substrates across biological membranes using the energy of ATP hydrolysis. Functional ABC proteins have two nucleotide-binding domains (NBDs) that bind and hydrolyze ATP, but the molecular mechanism of nucleotide hydrolysis is unresolved. This is due in part to the limited kinetic information on NBD association and dissociation. Here, we show dimerization of a catalytically active NBD and follow in real time the association and dissociation of NBDs from the changes in fluorescence emission of a tryptophan strategically located at the center of the dimer interface. Spectroscopic and structural studies demonstrated that the tryptophan can be used as dimerization probe, and we showed that under hydrolysis conditions (millimolar MgATP), not only the dimer dissociation rate increases, but also the dimerization rate. Neither dimer formation or dissociation are clearly favored, and the end result is a dynamic equilibrium where the concentrations of monomer and dimer are very similar. We proposed that based on their variable rates of hydrolysis, the rate-limiting step of the hydrolysis cycle may differ among full-length ABC proteins.
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