메뉴 건너뛰기




Volumn 332, Issue 1, 2003, Pages 229-242

Conformational changes in the multidrug transporter EmrE associated with substrate binding

Author keywords

Electron crystallography; Membrane protein; Multidrug resistance; Structure

Indexed keywords

CARBOHYDRATE DERIVATIVE; GLYCOPROTEIN P; LIPID; PROTEIN EMRE; TETRAPHENYLPHOSPHONIUM; UNCLASSIFIED DRUG;

EID: 0041735000     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00895-7     Document Type: Article
Times cited : (73)

References (28)
  • 1
    • 0036794327 scopus 로고    scopus 로고
    • Mechanistic parallels in bacterial and human multidrug efflux transporters
    • Zgurskaya H.I., Nikaido H. Mechanistic parallels in bacterial and human multidrug efflux transporters. Curr. Protein Pept. Sci. 3:2002;531-540.
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 531-540
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 2
    • 0029925159 scopus 로고    scopus 로고
    • The SMR family: A novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs
    • Paulsen I.T., Skurray R.A., Tam R., Saier M.H. Jr, Turner R.J., Weiner J.H., et al. The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs. Mol. Microbiol. 19:1996;1167-1175.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1167-1175
    • Paulsen, I.T.1    Skurray, R.A.2    Tam, R.3    Saier M.H., Jr.4    Turner, R.J.5    Weiner, J.H.6
  • 4
    • 0029999396 scopus 로고    scopus 로고
    • Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle
    • 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. 35:1996;7233-7238.
    • (1996) Biochemistry , vol.35 , pp. 7233-7238
    • Arkin, I.T.1    Russ, W.P.2    Lebendiker, M.3    Schuldiner, S.4
  • 6
    • 0035863057 scopus 로고    scopus 로고
    • The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 Å resolution
    • Tate C.G., Kunji E.R., Lebendiker M., Schuldiner S. The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 Å resolution. EMBO J. 20:2001;77-81.
    • (2001) EMBO J. , vol.20 , pp. 77-81
    • Tate, C.G.1    Kunji, E.R.2    Lebendiker, M.3    Schuldiner, S.4
  • 7
    • 0029856981 scopus 로고    scopus 로고
    • Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli
    • Yerushalmi H., Lebendiker M., Schuldiner S. Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli. J. Biol. Chem. 271:1996;31044-31048.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31044-31048
    • Yerushalmi, H.1    Lebendiker, M.2    Schuldiner, S.3
  • 8
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • Muth T.R., Schuldiner S. A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE. EMBO J. 19:2000;234-240.
    • (2000) EMBO J. , vol.19 , pp. 234-240
    • Muth, T.R.1    Schuldiner, S.2
  • 9
    • 0035930510 scopus 로고    scopus 로고
    • In vitro monomer swapping in EmrE, a multidrug transporter from Escherichia coli, reveals that the oligomer is the functional unit
    • 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. 276:2001;48243-48249.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48243-48249
    • Rotem, D.1    Sal-man, N.2    Schuldiner, S.3
  • 10
    • 0037126033 scopus 로고    scopus 로고
    • Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer
    • Soskine M., Steiner-Mordoch S., Schuldiner S. Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer. Proc. Natl Acad. Sci. USA. 99:2002;12043-12048.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12043-12048
    • Soskine, M.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 12
    • 0027970086 scopus 로고
    • Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump
    • Grinius L.L., Goldberg E.B. Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump. J. Biol. Chem. 269:1994;29998-30004.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29998-30004
    • Grinius, L.L.1    Goldberg, E.B.2
  • 13
    • 0034051663 scopus 로고    scopus 로고
    • An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli
    • Yerushalmi H., Schuldiner S. An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli. J. Biol. Chem. 275:2000;5264-5269.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5264-5269
    • Yerushalmi, H.1    Schuldiner, S.2
  • 14
    • 0035918237 scopus 로고    scopus 로고
    • A single carboxyl mutant of the multidrug transporter EmrE is fully functional
    • Yerushalmi H., Mordoch S.S., Schuldiner S. A single carboxyl mutant of the multidrug transporter EmrE is fully functional. J. Biol. Chem. 276:2001;12744-12748.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12744-12748
    • Yerushalmi, H.1    Mordoch, S.S.2    Schuldiner, S.3
  • 15
    • 0034733974 scopus 로고    scopus 로고
    • A common binding site for substrates and protons in EmrE, an ion-coupled multidrug transporter
    • Yerushalmi H., Schuldiner S. A common binding site for substrates and protons in EmrE, an ion-coupled multidrug transporter. FEBS Letters. 476:2000;93-97.
    • (2000) FEBS Letters , vol.476 , pp. 93-97
    • Yerushalmi, H.1    Schuldiner, S.2
  • 16
    • 0034610304 scopus 로고    scopus 로고
    • A model for coupling of H(+) and substrate fluxes based on "time-sharing" of a common binding site
    • Yerushalmi H., Schuldiner S. A model for coupling of H(+) and substrate fluxes based on "time-sharing" of a common binding site. Biochemistry. 39:2000;14711-14719.
    • (2000) Biochemistry , vol.39 , pp. 14711-14719
    • Yerushalmi, H.1    Schuldiner, S.2
  • 17
    • 0029788690 scopus 로고    scopus 로고
    • Identification of residues in the translocation pathway of EmrE, a multidrug antiporter from Escherichia coli
    • Lebendiker M., Schuldiner S. Identification of residues in the translocation pathway of EmrE, a multidrug antiporter from Escherichia coli. J. Biol. Chem. 271:1996;21193-21199.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21193-21199
    • Lebendiker, M.1    Schuldiner, S.2
  • 18
    • 0033516475 scopus 로고    scopus 로고
    • Scanning cysteine accessibility of EmrE, an H+-coupled multidrug transporter from Escherichia coli, reveals a hydrophobic pathway for solutes
    • 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. 274:1999;19480-19486.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19480-19486
    • Mordoch, S.S.1    Granot, D.2    Lebendiker, M.3    Schuldiner, S.4
  • 21
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S., Nakashima R., Yamashita E., Yamaguchi A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature. 419:2002;587-593.
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 22
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang G., Roth C.B. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science. 293:2001;1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 23
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher K.P., Lee A.T., Rees D.C. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science. 296:2002;1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 24
    • 17944370228 scopus 로고    scopus 로고
    • Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle
    • Rosenberg M.F., Velarde G., Ford R.C., Martin C., Berridge G., Kerr I.D., et al. Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle. EMBO J. 20:2001;5615-5625.
    • (2001) EMBO J. , vol.20 , pp. 5615-5625
    • Rosenberg, M.F.1    Velarde, G.2    Ford, R.C.3    Martin, C.4    Berridge, G.5    Kerr, I.D.6
  • 25
    • 0033594886 scopus 로고    scopus 로고
    • Bypassing the periplasm: Reconstitution of the AcrAB multidrug efflux pump of Escherichia coli
    • Zgurskaya H.I., Nikaido H. Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli. Proc. Natl Acad. Sci. USA. 96:1999;7190-7195.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7190-7195
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 26
    • 0033534178 scopus 로고    scopus 로고
    • The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids
    • Margolles A., Putman M., van Veen H.W., Konings W.N. The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids. Biochemistry. 38:1999;16298-16306.
    • (1999) Biochemistry , vol.38 , pp. 16298-16306
    • Margolles, A.1    Putman, M.2    Van Veen, H.W.3    Konings, W.N.4
  • 27
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner W., Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56:1973;502-514.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 28
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.