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Literature DB >> 16038903

Nucleotide binding to the homodimeric MJ0796 protein: a computational study of a prokaryotic ABC transporter NBD dimer.

Abstract

Transport by ABC proteins requires a cycle of ATP-driven conformational changes of the nucleotide binding domains (NBDs). We compare three molecular dynamics simulations of dimeric MJ0796: with ATP was present at both NBDs; with ATP at one NBD but ADP at the other; and without any bound ATP. In the simulation with ATP present at both NBDs, the dimeric protein interacts with the nucleotides in a symmetrical manner. However, if ADP is present at one binding site then both NBD-NBD and protein-ATP interactions are enhanced at the opposite site.

Entities: Chemical

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Year: 2005 PMID： 16038903 DOI： 10.1016/j.febslet.2005.06.027

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

10 in total

1. ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation.

Authors: Gang Lu; James M Westbrooks; Amy L Davidson; Jue Chen
Journal: Proc Natl Acad Sci U S A Date: 2005-12-02 Impact factor: 11.205

2. Simulation of the coupling between nucleotide binding and transmembrane domains in the ATP binding cassette transporter BtuCD.

Authors: Jacob Sonne; Christian Kandt; Günther H Peters; Flemming Y Hansen; Morten Ø Jensen; D Peter Tieleman
Journal: Biophys J Date: 2007-01-05 Impact factor: 4.033

3. 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.

Authors: Peter M Jones; Anthony M George
Journal: Biophys J Date: 2011-06-22 Impact factor: 4.033

9. The Nucleotide-Free State of the Multidrug Resistance ABC Transporter LmrA: Sulfhydryl Cross-Linking Supports a Constant Contact, Head-to-Tail Configuration of the Nucleotide-Binding Domains.

Authors: Peter M Jones; Anthony M George
Journal: PLoS One Date: 2015-06-29 Impact factor: 3.240

10. Insights into how nucleotide-binding domains power ABC transport.

Authors: Simon Newstead; Philip W Fowler; Paul Bilton; Elisabeth P Carpenter; Peter J Sadler; Dominic J Campopiano; Mark S P Sansom; So Iwata
Journal: Structure Date: 2009-09-09 Impact factor: 5.006

10 in total

Nucleotide binding to the homodimeric MJ0796 protein: a computational study of a prokaryotic ABC transporter NBD dimer.

1. ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation.

2. Simulation of the coupling between nucleotide binding and transmembrane domains in the ATP binding cassette transporter BtuCD.

3. 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.

4. Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F.

5. In silico model for P-glycoprotein substrate prediction: insights from molecular dynamics and in vitro studies.

Review 6. Structure, function, and evolution of bacterial ATP-binding cassette systems.

7. Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis.

8. Inter-domain communication mechanisms in an ABC importer: a molecular dynamics study of the MalFGK2E complex.

9. The Nucleotide-Free State of the Multidrug Resistance ABC Transporter LmrA: Sulfhydryl Cross-Linking Supports a Constant Contact, Head-to-Tail Configuration of the Nucleotide-Binding Domains.

10. Insights into how nucleotide-binding domains power ABC transport.