ArticleBiophysical journal2008
Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- ATP hydrolysis and nucleotide exit enhance maltose translocation in the MalFGKScientific reports · 2021Article
- Conformational changes in the nucleotide-binding domains of P-glycoprotein induced by ATP hydrolysis.FEBS letters · 2021Article
- Conversion of chemical to mechanical energy by the nucleotide binding domains of ABCB1.Scientific reports · 2020Article
- Comparison of mechanistic transport cycle models of ABC exporters.Biochimica et biophysica acta. Biomembranes · 2018Review
- Dissecting the Forces that Dominate Dimerization of the Nucleotide Binding Domains of ABCB1.Biophysical journal · 2018Article
- Cell envelope stress in mycobacteria is regulated by the novel signal transduction ATPase IniR in response to trehalose.PLoS genetics · 2017Article
- Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F.Biophysical journal · 2016Article
- ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations.PloS one · 2016Article
- Toward Determining ATPase Mechanism in ABC Transporters: Development of the Reaction Path-Force Matching QM/MM Method.Methods in enzymology · 2016Article
- Article
- In silico screening for inhibitors of p-glycoprotein that target the nucleotide binding domains.Molecular pharmacology · 2014Article
- 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
- Mechanistic picture for conformational transition of a membrane transporter at atomic resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- In silico model for P-glycoprotein substrate prediction: insights from molecular dynamics and in vitro studies.Journal of computer-aided molecular design · 2013Article
- Visualizing functional motions of membrane transporters with molecular dynamics simulations.Biochemistry · 2013Review
- Molecular dynamics simulations of membrane proteins.Biophysical reviews · 2012Review
- Conformational coupling of the nucleotide-binding and the transmembrane domains in ABC transporters.Biophysical journal · 2011Article
- Inter-domain communication mechanisms in an ABC importer: a molecular dynamics study of the MalFGK2E complex.PLoS computational biology · 2011Article
- Structural consequences of ATP hydrolysis on the ABC transporter NBD dimer: molecular dynamics studies of HlyB.Protein science : a publication of the Protein Society · 2011Article
- Molecular-dynamics simulations of the ATP/apo state of a multidrug ATP-binding cassette transporter provide a structural and mechanistic basis for the asymmetric occluded state.Biophysical journal · 2011Article
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2 authors.
Funding
Abstract
ABC transporters constitute one of the most abundant membrane transporter families. The most common feature shared in the family is the highly conserved nucleotide binding domains (NBDs) that drive the transport process through binding and hydrolysis of ATP. Molecular dynamics simulations are used to investigate the effect of ATP hydrolysis in the NBDs. Starting with the ATP-bound, closed dimer of MalK, four simulation systems with all possible combinations of ATP or ADP-P(i) bound to the two nucleotide binding sites are constructed and simulated with equilibrium molecular dynamics for approximately 70 ns each. The results suggest that the closed form of the NBD dimer can only be maintained with two bound ATP molecules; in other words, hydrolysis of one ATP can lead to the opening of the dimer interface of the NBD dimer. Furthermore, we observed that the opening is an immediate effect of hydrolysis of ATP into ADP and P(i) rather than the dissociation of hydrolysis products. In addition, the opening is mechanistically triggered by the dissociation of the LSGGQ motif from the bound nucleotide. A metastable ADP-P(i) bound conformational state is consistently observed before the dimer opening in all the simulation systems.
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