ArticleActa crystallographica. Section D, Biological crystallography2009
An emerging consensus for the structure of EmrE.
Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed.
- Functional Role of YnfA, an Efflux Transporter in Resistance to Antimicrobial Agents in Shigella flexneri.Antimicrobial agents and chemotherapy · 2022Article
- General principles of secondary active transporter function.Biophysics reviews · 2022Review
- Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021Review
- Structural Insights into Transporter-Mediated Drug Resistance in Infectious Diseases.Journal of molecular biology · 2021Review
- Electrostatic lock in the transport cycle of the multidrug resistance transporter EmrE.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Few Conserved Amino Acids in the Small Multidrug Resistance Transporter EmrE Influence Drug Polyselectivity.Antimicrobial agents and chemotherapy · 2018Article
- Article
- Biocide Selective TolC-Independent Efflux Pumps in Enterobacteriaceae.The Journal of membrane biology · 2018Article
- Mistic's membrane association and its assistance in overexpression of a human GPCR are independent processes.Protein science : a publication of the Protein Society · 2015Article
- Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014Review
- Combination of ¹⁵N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrE.Journal of biomolecular NMR · 2013Article
- Mass spectrometry--from peripheral proteins to membrane motors.Journal of molecular biology · 2012Review
- Analyzing conformational changes in the transport cycle of EmrE.Current opinion in structural biology · 2012Review
- Article
- A novel metal transporter mediating manganese export (MntX) regulates the Mn to Fe intracellular ratio and Neisseria meningitidis virulence.PLoS pathogens · 2011Article
- Functional specialization in nucleotide sugar transporters occurred through differentiation of the gene cluster EamA (DUF6) before the radiation of Viridiplantae.BMC evolutionary biology · 2011Article
- 1H, 13C, 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation.Biomolecular NMR assignments · 2010Article
- Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals.Structure (London, England : 1993) · 2010Article
- Review
- Diversity and evolution of the small multidrug resistance protein family.BMC evolutionary biology · 2009Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The archetypical member of the small multidrug-resistance family is EmrE, a multidrug transporter that extrudes toxic polyaromatic cations from the cell coupled to the inward movement of protons down a concentration gradient. The architecture of EmrE was first defined from the analysis of two-dimensional crystals by cryoelectron microscopy (cryo-EM), which showed that EmrE was an unusual asymmetric dimer formed from a bundle of eight alpha-helices. The most favoured interpretation of the structure was that the monomers were oriented in opposite orientations in the membrane in an antiparallel orientation. A model was subsequently built based upon the cryo-EM data and evolutionary constraints and this model was consistent with mutagenic data indicating which amino-acid residues were important for substrate binding and transport. Two X-ray structures that differed significantly from the cryo-EM structure were subsequently retracted owing to a data-analysis error. However, the revised X-ray structure with substrate bound is extremely similar to the model built from the cryo-EM structure (r.m.s.d. of 1.4 A), suggesting that the proposed antiparallel orientation of the monomers is indeed correct; this represents a new structural paradigm in membrane-protein structures. The vast majority of mutagenic and biochemical data corroborate this structure, although cross-linking studies and recent EPR data apparently support a model of EmrE that contains parallel dimers.
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