ArticleBiophysical journal2004
A structural model of EmrE, a multi-drug transporter from Escherichia coli.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 33 citations in OpenAlex.
- Role of bacterial efflux pumps in antibiotic resistance, virulence, and strategies to discover novel efflux pump inhibitors.Microbiology (Reading, England) · 2023Review
- Functional Role of YnfA, an Efflux Transporter in Resistance to Antimicrobial Agents in Shigella flexneri.Antimicrobial agents and chemotherapy · 2022Article
- Plant glucose transporter structure and function.Pflugers Archiv : European journal of physiology · 2020Review
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structure, dynamics, and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes.The Journal of biological chemistry · 2010Article
- Sequence alignment and homology threading reveals prokaryotic and eukaryotic proteins similar to lactose permease.Journal of molecular biology · 2006Article
- Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily.Biophysical journal · 2006Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Using a recently reported computational method, we describe an approach to model the structure of EmrE, a proton coupled multi-drug transporter of Escherichia coli. EmrE is the smallest ion-coupled transporter known; it functions as an oligomer and each monomer comprises four transmembrane segments. Because of its size, EmrE provides a unique experimental paradigm. The computational method does not afford a unique solution for the monomer. The experimental constraints available were used to select the most likely structure and to dock two monomers together to yield a dimer. The model is further validated by modeling of Hsmr, an EmrE homolog with a remarkable amino acid composition with over 40% of Ala and Val. The Hsmr model is similar to that of EmrE, with the majority of the Ala or Val residues facing the lipid. In addition, the model of EmrE features a putative substrate-binding site very similar to that observed in BmrR, a transcription activator of multi-drug transporters, with a similar substrate profile. The two crucial residues that couple proton fluxes with substrate binding in the homo-dimer of EmrE, Glu-14, have a spatial arrangement that agrees with proposed molecular mechanisms of transport.
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