ArticleThe Biochemical journal2005
Positive co-operative activity and dimerization of the isolated ABC ATPase domain of HlyB from Escherichia coli.
Article in The Biochemical journal, 2005. 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, 35 citations in OpenAlex.
- Type 1 secretion necessitates a tight interplay between all domains of the ABC transporter.Scientific reports · 2024Article
- Article
- The role of the degenerate nucleotide binding site in type I ABC exporters.FEBS letters · 2020Review
- Characterization of the nucleotide-binding domain NsrF from the BceAB-type ABC-transporter NsrFP from the human pathogen Streptococcus agalactiae.Scientific reports · 2020Article
- The crystal structure of Klebsiella pneumoniae FeoA reveals a site for protein-protein interactions.Proteins · 2019Article
- Purification and characterisation of the yeast plasma membrane ATP binding cassette transporter Pdr11p.PloS one · 2017Article
- Type I Protein Secretion-Deceptively Simple yet with a Wide Range of Mechanistic Variability across the Family.EcoSal Plus · 2016Review
- ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism.Nature structural & molecular biology · 2015Article
- Time-resolved Fourier transform infrared spectroscopy of the nucleotide-binding domain from the ATP-binding Cassette transporter MsbA: ATP hydrolysis is the rate-limiting step in the catalytic cycle.The Journal of biological chemistry · 2012Article
- Potassium-activated GTPase reaction in the G Protein-coupled ferrous iron transporter B.The Journal of biological chemistry · 2010Article
- The H-loop in the second nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator is required for efficient chloride channel closing.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2010Article
- Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis.Biophysical journal · 2008Article
- Molecular basis for differential nucleotide binding of the nucleotide-binding domain of ABC-transporter CvaB.Biochemistry · 2006Article
- Nucleotide-dependent dimerization of the C-terminal domain of the ABC transporter CvaB in colicin V secretion.Journal of bacteriology · 2006Article
- Attempts to characterize the NBD heterodimer of MRP1: transient complex formation involves Gly771 of the ABC signature sequence but does not enhance the intrinsic ATPase activity.The Biochemical journal · 2005Article
- H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB.The EMBO journal · 2005Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ATPase activity of the ABC (ATP-binding cassette) ATPase domain of the HlyB (haemolysin B) transporter is required for secretion of Escherichia coli haemolysin via the type I pathway. Although ABC transporters are generally presumed to function as dimers, the precise role of dimerization remains unclear. In the present study, we have analysed the HlyB ABC domain, purified separately from the membrane domain, with respect to its activity and capacity to form physically detectable dimers. The ATPase activity of the isolated ABC domain clearly demonstrated positive co-operativity, with a Hill coefficient of 1.7. Furthermore, the activity is (reversibly) inhibited by salt concentrations in the physiological range accompanied by proportionately decreased binding of 8-azido-ATP. Inhibition of activity with increasing salt concentration resulted in a change in flexibility as detected by intrinsic tryptophan fluorescence. Finally, ATPase activity was sensitive towards orthovanadate, with an IC50 of 16 microM, consistent with the presence of transient dimers during ATP hydrolysis. Nevertheless, over a wide range of protein or of NaCl or KCl concentrations, the ABC ATPase was only detected as a monomer, as measured by ultracentrifugation or gel filtration. In contrast, in the absence of salt, the sedimentation velocity determined by analytical ultracentrifugation suggested a rapid equilibrium between monomers and dimers. Small amounts of dimers, but apparently only when stabilized by 8-azido-ATP, were also detected by gel filtration, even in the presence of salt. These data are consistent with the fact that monomers can interact at least transiently and are the important species during ATP hydrolysis.
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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.