ArticleThe Journal of biological chemistry2012
Dissociation of ATP-binding cassette nucleotide-binding domain dimers into monomers during the hydrolysis cycle.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- ABCG2 transporter: Structural and functional associations with gout (Review).International journal of molecular medicine · 2026Review
- Conformational equilibrium of an ABC transporter analyzed by luminescence resonance energy transfer.Biophysical journal · 2025Article
- Article
- The molecular evolution of function in the CFTR chloride channel.The Journal of general physiology · 2021Article
- ABC Exporters in Pathogenesis: Role of Synthetic Anti-Microbial Peptides.The protein journal · 2020Article
- Adjacent mutations in the archaeal Rad50 ABC ATPase D-loop disrupt allosteric regulation of ATP hydrolysis through different mechanisms.Nucleic acids research · 2020Article
- 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
- Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.The Journal of biological chemistry · 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
- 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
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ATP-binding cassette (ABC) proteins have two nucleotide-binding domains (NBDs) that work as dimers to bind and hydrolyze ATP, but the molecular mechanism of nucleotide hydrolysis is controversial. In particular, it is still unresolved whether hydrolysis leads to dissociation of the ATP-induced dimers or opening of the dimers, with the NBDs remaining in contact during the hydrolysis cycle. We studied a prototypical ABC NBD, the Methanococcus jannaschii MJ0796, using spectroscopic techniques. We show that fluorescence from a tryptophan positioned at the dimer interface and luminescence resonance energy transfer between probes reacted with single-cysteine mutants can be used to follow NBD association/dissociation in real time. The intermonomer distances calculated from luminescence resonance energy transfer data indicate that the NBDs separate completely following ATP hydrolysis, instead of opening. The results support ABC protein NBD association/dissociation, as opposed to constant-contact models.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.