ArticleProteins2012
Simulations of substrate transport in the multidrug transporter EmrD.
Article in Proteins, 2012. 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.
- Unveiling Antibiotic Resistance: Genome Sequencing of Streptomycin-ResistantMicroorganisms · 2024Article
- Major facilitator superfamily efflux pumps in human pathogens: Role in multidrug resistance and beyond.Current research in microbial sciences · 2024Article
- The role of TMS 12 in the staphylococcal multidrug efflux protein QacA.The Journal of antimicrobial chemotherapy · 2023Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Functional and Structural Roles of the Major Facilitator Superfamily Bacterial Multidrug Efflux Pumps.Microorganisms · 2020Review
- Article
- Insight into determinants of substrate binding and transport in a multidrug efflux protein.Scientific reports · 2016Article
- Flexible gates generate occluded intermediates in the transport cycle of LacY.Journal of molecular biology · 2014Article
- Protonation drives the conformational switch in the multidrug transporter LmrP.Nature chemical biology · 2014Article
- Structure and pH-induced structural rearrangements of the putative multidrug efflux pump EmrD in liposomes probed by site-directed spin labeling.Biochemistry · 2013Article
- Proton-coupled dynamics in lactose permease.Structure (London, England : 1993) · 2012Article
- Structural comparison of bacterial multidrug efflux pumps of the major facilitator superfamily.Trends in cell & molecular biologyArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
EmrD is a multidrug resistance (MDR) transporter from Escherichia coli, which is involved in the efflux of amphipathic compounds from the cytoplasm, and the first MDR member of the major facilitator superfamily to be crystallized. Molecular dynamics simulation of EmrD in a phospholipid bilayer was used to characterize the conformational dynamics of the protein. Motions that support a previously proposed lateral diffusion pathway for substrate from the cytoplasmic membrane leaflet into the EmrD central cavity were observed. In addition, the translocation pathway of meta-chloro carbonylcyanide phenylhydrazone (CCCP) was probed using both standard and steered molecular dynamics simulation. In particular, interactions of a few specific residues with CCCP have been identified. Finally, a large motion of two residues, Val 45 and Leu 233, was observed with the passage of CCCP into the periplasmic space, placing a lower bound on the extent of opening required at this end of the protein for substrate transport. Overall, our simulations probe details of the transport pathway, motions of EmrD at an atomic level of detail, and offer new insights into the functioning of MDR transporters.
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Registered trials
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.