ArticleProceedings of the National Academy of Sciences of the United States of America2005
ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
68 citing papers in PubMed, 134 citations in OpenAlex.
- Single-molecule dynamics reveal ATP binding alone powers substrate translocation by an ABC transporter.Nature communications · 2026Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- Structurally diverse C-terminal accessory domains in type I ABC importers reveal distinct regulatory mechanisms.Structure (London, England : 1993) · 2025Review
- Article
- Urea transport and hydrolysis in the rumen: A review.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2021Review
- Molecular basis of cholesterol efflux via ABCG subfamily transporters.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability.Scientific reports · 2020Article
- Dissecting the Forces that Dominate Dimerization of the Nucleotide Binding Domains of ABCB1.Biophysical journal · 2018Article
- Sulfate Transporters in Dissimilatory Sulfate Reducing Microorganisms: A Comparative Genomics Analysis.Frontiers in microbiology · 2018Review
- Direct Spectroscopic Detection of ATP Turnover Reveals Mechanistic Divergence of ABC Exporters.Structure (London, England : 1993) · 2017Article
- Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalKThe Journal of biological chemistry · 2017Article
- The uncoupled ATPase activity of the ABC transporter BtuC2D2 leads to a hysteretic conformational change, conformational memory, and improved activity.Scientific reports · 2016Article
- Sequential Action of MalE and Maltose Allows Coupling ATP Hydrolysis to Translocation in the MalFGK2 Transporter.The Journal of biological chemistry · 2015Article
- Characterizing the binding interactions between P-glycoprotein and eight known cardiovascular transport substrates.Pharmacology research & perspectives · 2015Article
- Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8.Journal of structural and functional genomics · 2014Article
- Structural diversity of ABC transporters.The Journal of general physiology · 2014Review
- Analyses of conformational states of the transporter associated with antigen processing (TAP) protein in a native cellular membrane environment.The Journal of biological chemistry · 2013Article
- Carbohydrate kinase (RhaK)-dependent ABC transport of rhamnose in Rhizobium leguminosarum demonstrates genetic separation of kinase and transport activities.Journal of bacteriology · 2013Article
- Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
8 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
ATP-binding cassette (ABC) transporters couple ATP binding and hydrolysis to the movement of substances across the membrane; conformational changes clearly play an important role in the transporter mechanism. Previously, we have shown that a dimer of MalK, the ATPase subunit of the maltose transporter from Escherichia coli, undergoes a tweezers-like motion in a transport cycle. The MalK monomer consists of an N-terminal nucleotide binding domain and a C-terminal regulatory domain. The two nucleotide-binding domains in a dimer are either open or closed, depending on whether ATP is present, while the regulatory domains maintain contacts to hold the dimer together. In this work, the structure of MalK in a posthydrolysis state is presented, obtained by cocrystallizing MalK with ATP-Mg(2+). ATP was hydrolyzed in the crystallization drop, and ADP-Mg(2+) was found in the resulting crystal structure. In contrast to the ATP-bound form where two ATP molecules are buried in a closed interface between the nucleotide-binding domains, the two nucleotide-binding domains of the ADP-bound form are open, indicating that ADP, unlike ATP, cannot stabilize the closed form. This conclusion is further supported by oligomerization studies of MalK in solution. At low protein concentrations, ATP promotes dimerization of MalK, whereas ADP does not. The structures of dimeric MalK in the nucleotide-free, ATP-bound, and ADP-bound forms provide a framework for understanding the nature of the conformational changes that occur in an ATP-binding cassette transporter hydrolysis cycle, as well as how conformational changes in MalK are coupled to solute transport.
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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.