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Antiparallel EmrE exports drugs by exchanging between asymmetric structures

Morrison, Emma A., DeKoster, Gregory T., Dutta, Supratik, Vafabakhsh, Reza, Clarkson, Michael W., Bahl, Arjun, Kern, Dorothee, Ha, Taekjip, Henzler-Wildman, Katherine A.·2012·Nature
DOI 10.1038/nature10703PMC PMC3253143
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  • Dual-topology dimeric construction is known in small multidrug transporters but has not been previously observed in ion channels.

    “Dual-topology dimeric construction is known in small multidrug transporters9–11 but has not been previously observed in ion channels.”

    From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [11]

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Research works printed but not linked: 48

  1. Arkin, I. T., Russ, W. P., Lebendiker, M. & Schuldiner, S. Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle. Biochemistry 35, 7233–7238 (1996) · DOI
  2. Yerushalmi, H., Lebendiker, M. & Schuldiner, S. EmrE, an Escherichia coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents. J. Biol. Chem. 270, 6856–6863 (1995) · DOI
  3. Schuldiner, S. EmrE, a model for studying evolution and mechanism of ion-coupled transporters. Biochim. Biophys. Acta 1794, 748–762 (2009) · DOI · Paper page
  4. Tate, C. G., Ubarretxena-Belandia, I. & Baldwin, J. M. Conformational changes in the multidrug transporter EmrE associated with substrate binding. J. Mol. Biol. 332, 229–242 (2003) · DOI
  5. Butler, P. J., Ubarretxena-Belandia, I., Warne, T. & Tate, C. G. The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state. J. Mol. Biol. 340, 797–808 (2004) · DOI
  6. Ubarretxena-Belandia, I. & Tate, C. G. New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: an unusual asymmetric homo-dimer. FEBS Lett. 564, 234–238 (2004) · DOI
  7. Chen, Y. J. et al. X-ray structure of EmrE supports dual topology model. Proc. Natl Acad. Sci. USA 104, 18999–19004 (2007) · DOI
  8. Ninio, S., Elbaz, Y. & Schuldiner, S. The membrane topology of EmrE – a small multidrug transporter from Escherichia coli . FEBS Lett. 562, 193–196 (2004) · DOI
  9. Rapp, M., Seppälä, S., Granseth, E. & von Heijne, G. Emulating membrane protein evolution by rational design. Science 315, 1282–1284 (2007) · DOI
  10. McHaourab, H. S., Mishra, S., Koteiche, H. A. & Amadi, S. H. Role of sequence bias in the topology of the multidrug transporter EmrE. Biochemistry 47, 7980–7982 (2008) · DOI
  11. Steiner-Mordoch, S. et al. Parallel topology of genetically fused EmrE homodimers. EMBO J. 27, 17–26 (2008) · DOI
  12. Korkhov, V. M. & Tate, C. G. An emerging consensus for the structure of EmrE. Acta Crystallogr. D 65, 186–192 (2009) · DOI
  13. Amadi, S. T., Koteiche, H. A., Mishra, S. & McHaourab, H. S. Structure, dynamics and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes. J. Biol. Chem. 285, 26710–26718 (2010) · DOI
  14. Soskine, M., Mark, S., Tayer, N., Mizrachi, R. & Schuldiner, S. On parallel and antiparallel topology of a homodimeric multidrug transporter. J. Biol. Chem. 281, 36205–36212 (2006) · DOI
  15. Charalambous, K., Miller, D., Curnow, P. & Booth, P. J. Lipid bilayer composition influences small multidrug transporters. BMC Biochem. 9, 31 (2008) · DOI
  16. Seppala, S., Slusky, J., Lloris-Garcera, P., Rapp, M. & Von Heijne, G. Control of membrane protein topology by a single C-terminal residue. Science 328, 1698–1700 (2010) · DOI
  17. Nasie, I., Steiner-Mordoch, S., Gold, A. & Schuldiner, S. Topologically random insertion of EmrE supports a pathway for evolution of inverted repeats in ion-coupled transporters. J. Biol. Chem. 285, 15234–15244 (2010) · DOI
  18. Fleishman, S. J. et al. Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain. J. Mol. Biol. 364, 54–67 (2006) · DOI
  19. Yerushalmi, H. & Schuldiner, S. A model for coupling of H+ and substrate fluxes based on ‘time-sharing’ of a common binding site. Biochemistry 39, 14711–14719 (2000) · DOI
  20. Adam, Y., Tayer, N., Rotem, D., Schreiber, G. & Schuldiner, S. The fast release of sticky protons: kinetics of substrate binding and proton release in a multidrug transporter. Proc. Natl Acad. Sci. USA 104, 17989–17994 (2007) · DOI
  21. Jardetzky, O. Simple allosteric model for membrane pumps. Nature 211, 969–970 (1966) · DOI
  22. West, I. C. Ligand conduction and the gated-pore mechanism of transmembrane transport. Biochim. Biophys. Acta 1331, 213–234 (1997) · DOI
  23. Glover, K. J. et al. Structural evaluation of phospholipid bicelles for solution-state studies of membrane-associated biomolecules. Biophys. J. 81, 2163–2171 (2001) · DOI
  24. Whiles, J., Ceems, R. & Vold, R. Bicelles in structure–function studies of membrane-associated proteins. Bioorg. Chem. 30, 431–442 (2002) · DOI
  25. Raschle, T., Hiller, S., Etzkorn, M. & Wagner, G. Nonmicellar systems for solution NMR spectroscopy of membrane proteins. Curr. Opin. Struct. Biol. 20, 471–479 (2010) · DOI
  26. Lehner, I. et al. The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric. J. Biol. Chem. 283, 3281–3288 (2008) · DOI
  27. Ubarretxena-Belandia, I., Baldwin, J. M., Schuldiner, S. & Tate, C. G. Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer. EMBO J. 22, 6175–6181 (2003) · DOI · Paper page
  28. Rotem, D. & Schuldiner, S. EmrE, a multidrug transporter from Escherichia coli, transports monovalent and divalent substrates with the same stoichiometry. J. Biol. Chem. 279, 48787–48793 (2004) · DOI
  29. Soskine, M., Adam, Y. & Schuldiner, S. Direct evidence for substrate-induced proton release in detergent-solubilized EmrE, a multidrug transporter. J. Biol. Chem. 279, 9951–9955 (2004) · DOI
  30. Yerushalmi, H., Mordoch, S. S. & Schuldiner, S. A single carboxyl mutant of the multidrug transporter EmrE is fully functional. J. Biol. Chem. 276, 12744–12748 (2001) · DOI
  31. Muth, T. R. & Schuldiner, S. A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE. EMBO J. 19, 234–240 (2000) · DOI
  32. Sanders, C. R. & Sönnichsen, F. Solution NMR of membrane proteins: practice and challenges. Magn. Reson. Chem 44 (NMR of Proteins in Solution special issue). S24–S40 (2006) · DOI
  33. Miller, D. et al. In vitro unfolding and refolding of the small multidrug transporter EmrE. J. Mol. Biol. 393, 815–832 (2009) · DOI
  34. Sikora, C. W. & Turner, R. J. Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry. Biophys. J. 88, 475–482 (2005) · DOI
  35. Li, Y. & Palmer, A. G. TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins. J. Biomol. Nucl. Magn. Reson. 45, 357–360 (2009)
  36. Farrow, N. A., Zhang, O., Forman-Kay, J. D. & Kay, L. E. A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium. J. Biomol. Nucl. Magn. Reson. 4, 727–734 (1994)
  37. Miloushev, V. Z. et al. Dynamic properties of a type II cadherin adhesive domain: implications for the mechanism of strand-swapping of classical cadherins. Structure 16, 1195–1205 (2008) · DOI
  38. Nara, T. et al. Anti-parallel membrane topology of a homo-dimeric multidrug transporter, EmrE. J. Biochem. 142, 621–625 (2007) · DOI
  39. Korkhov, V. M. & Tate, C. G. Electron crystallography reveals plasticity within the drug binding site of the small multidrug transporter EmrE. J. Mol. Biol. 377, 1094–1103 (2008) · DOI
  40. Agarwal, V., Fink, U., Schuldiner, S. & Reif, B. MAS solid-state NMR studies on the multidrug transporter EmrE. Biochim. Biophys. Acta 1768, 3036–3043 (2007) · DOI
  41. Mordoch, S. S., Granot, D., Lebendiker, M. & Schuldiner, S. Scanning cysteine accessibility of EmrE, an H+-coupled multidrug transporter from Escherichia coli, reveals a hydrophobic pathway for solutes. J. Biol. Chem. 274, 19480–19486 (1999) · DOI
  42. Ha, T. et al. Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl Acad. Sci. USA 93, 6264–6268 (1996) · DOI
  43. Roy, R., Hohng, S. & Ha, T. A practical guide to single-molecule FRET. Nature Methods 5, 507–516 (2008) · DOI
  44. Sharoni, M., Steiner-Mordoch, S. & Schuldiner, S. Exploring the binding domain of EmrE, the smallest multidrug transporter. J. Biol. Chem. 280, 32849–32855 (2005) · DOI
  45. Weinglass, A. B. et al. Exploring the role of a unique carboxyl residue in EmrE by mass spectrometry. J. Biol. Chem. 280, 7487–7492 (2005) · DOI
  46. Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. Nucl. Magn. Reson. 6, 277–293 (1995)
  47. Johnson, B. A. & Blevins, R. A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. Nucl. Magn. Reson. 4, 603–614 (1994)
  48. Rotem, D., Sal-man, N. & Schuldiner, S. In vitro monomer swapping in EmrE, a multidrug transporter from Escherichia coli, reveals that the oligomer is the functional unit. J. Biol. Chem. 276, 48243–48249 (2001) · DOI

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Metadata

Authors
Morrison, E. A., DeKoster, G. T., Dutta, S., Vafabakhsh, R., Clarkson, M. W., Bahl, A., Kern, D., Ha, T., & Henzler-Wildman, K. A.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2011-12-18
Volume
481
Issue
7379
Pages
45-50
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature10703
PMC
PMC3253143
Cited by
215
References
0
Language
en
Licence
www.springer.com/tdm (tdm)

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