ArticleBiophysical journal2006
Molecular dynamics simulations of E. coli MsbA transmembrane domain: formation of a semipore structure.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Switching Cytolytic Nanopores into Antimicrobial Fractal Ruptures by a Single Side Chain Mutation.ACS nano · 2021Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Tuneable poration: host defense peptides as sequence probes for antimicrobial mechanisms.Scientific reports · 2018Article
- Review
- Membrane association of the bacterial riboregulator Hfq and functional perspectives.Scientific reports · 2017Article
- Engineering monolayer poration for rapid exfoliation of microbial membranes.Chemical science · 2017Article
- In silico analysis of the binding of anthelmintics to Caenorhabditis elegansP-glycoprotein 1.International journal for parasitology. Drugs and drug resistance · 2016Article
- Spontaneous Reconstitution of Functional Transmembrane Proteins During Bioorthogonal Phospholipid Membrane Synthesis.Angewandte Chemie (International ed. in English) · 2015Article
- Inter-domain communication mechanisms in an ABC importer: a molecular dynamics study of the MalFGK2E complex.PLoS computational biology · 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
- Molecular dynamics simulations and membrane protein structure quality.European biophysics journal : EBJ · 2008Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human P-glycoprotein (MDR1/P-gp) is an ATP-binding cassette (ABC) transporter involved in cellular response to chemical stress and failures of anticancer chemotherapy. In the absence of a high-resolution structure for P-gp, we were interested in the closest P-gp homolog for which a crystal structure is available: the bacterial ABC transporter MsbA. Here we present the molecular dynamics simulations performed on the transmembrane domain of the open-state MsbA in a bilayer composed of palmitoyl oleoyl phosphatidylethanolamine lipids. The system studied contained more than 90,000 atoms and was simulated for 50 ns. This simulation shows that the open-state structure of MsbA can be stable in a membrane environment and provides invaluable insights into the structural relationships between the protein and its surrounding lipids. This study reveals the formation of a semipore-like structure stabilized by two key phospholipids which interact with the hinge region of the protein during the entire simulation. Multiple sequence alignments of ABC transporters reveal that one of the residues involved in the interaction with these two phospholipids are under a strong selection pressure specifically applied on the bacterial homologs of MsbA. Hence, comparison of molecular dynamics simulation and phylogenetic data appears as a powerful approach to investigate the functional relevance of molecular events occurring during simulations.
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