ArticleThe Journal of biological chemistry2008
Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 53 citations in OpenAlex.
- Protonated Structure of EmrE Reveals C-terminal Tail Gating Mechanism.bioRxiv : the preprint server for biology · 2026Article
- Antimicrobial and Antibiofilm Activities of Glycyl-Histidine and Methionyl-Glycine Dipeptides: In Vitro and Molecular Docking Studies.Molecules (Basel, Switzerland) · 2026Article
- Design principles of the common Gly-X6-Gly membrane protein building block.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Novel small multidrug resistance protein Tmt endows the Escherichia coli with triphenylmethane dyes bioremediation capability.Biotechnology letters · 2024Article
- De novo-designed transmembrane proteins bind and regulate a cytokine receptor.Nature chemical biology · 2024Article
- Dynamics underlie the drug recognition mechanism by the efflux transporter EmrE.Nature communications · 2024Article
- TrhA, a bacterial progestin and adiponectin receptor homolog, couples membrane energetics homeostasis and unsaturated fatty acid metabolism.Journal of bacteriology · 2024Article
- Still rocking in the structural era: A molecular overview of the small multidrug resistance (SMR) transporter family.The Journal of biological chemistry · 2022Review
- Cotranslational folding and assembly of the dimericProceedings of the National Academy of Sciences of the United States of America · 2022Article
- High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport.Nature communications · 2022Article
- Membrane orientation and oligomerization of the melanocortin receptor accessory protein 2.The Journal of biological chemistry · 2020Article
- Identification of an Alternating-Access Dynamics Mutant of EmrE with Impaired Transport.Journal of molecular biology · 2019Article
- The C terminus of the bacterial multidrug transporter EmrE couples drug binding to proton release.The Journal of biological chemistry · 2018Article
- Structure of theProceedings 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
- Stable membrane orientations of small dual-topology membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A conserved OmpA-like protein in Legionella pneumophila required for efficient intracellular replication.FEMS microbiology letters · 2016Article
- Optimization of RGD-Containing Cyclic Peptides against αvβ3 Integrin.Molecular cancer therapeutics · 2016Article
- Efflux by small multidrug resistance proteins is inhibited by membrane-interactive helix-stapled peptides.The Journal of biological chemistry · 2015Article
- A structured loop modulates coupling between the substrate-binding and dimerization domains in the multidrug resistance transporter EmrE.The Journal of biological chemistry · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Glycine residues may play functional and structural roles in membrane proteins. In this work we studied the role of glycine residues in EmrE, a small multidrug transporter from Escherichia coli. EmrE extrudes various drugs across the plasma membrane in exchange with protons and, as a result, confers resistance against their toxic effects. Each of 12 glycine residues was replaced by site-directed mutagenesis. Four of the 12 glycine residues in EmrE are evolutionary conserved within the small multidrug resistance family of multidrug transporters. Our analysis reveals that only two (Gly-67 and Gly-97) of these four highly conserved residues are essential for transporter activity. Moreover, two glycine positions that are less conserved, Gly-17 and Gly-90, demonstrate also a nil phenotype when substituted. Our present results identifying Gly-17 and Gly-67 as irreplaceable reinforce the importance of previously defined functional clusters. Two essential glycine residues, Gly-90 and Gly-97, form a protein motif in which glycine residues are separated by six other residues (GG7). Upon substitution of glycine in these positions, the protein ability to form dimers is impaired as evaluated by cross-linking and pull-down experiments.
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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.