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Volumn 74, Issue 5, 2007, Pages 672-678

New structure model for the ATP-binding cassette multidrug transporter LmrA

Author keywords

ABC transporter; Cysteine cross linking; Homology modelling; LmrA; Multidrug resistance; Sav1866

Indexed keywords

ABC TRANSPORTER; ATP BINDING CASSETTE TRANSPORTER LMRA; CYSTEINE; HOMODIMER; MERCAPTOETHANOL; MSBA PROTEIN; UNCLASSIFIED DRUG;

EID: 34447626315     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2007.05.015     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 34147214716 scopus 로고    scopus 로고
    • Multiple molecular mechanisms for multidrug resistance transporters
    • Higgins C.F. Multiple molecular mechanisms for multidrug resistance transporters. Nature 446 (2007) 749-757
    • (2007) Nature , vol.446 , pp. 749-757
    • Higgins, C.F.1
  • 2
    • 1842610700 scopus 로고    scopus 로고
    • The ABC transporter structure and mechanism: perspectives on recent research
    • Jones P.M., and George A.M. The ABC transporter structure and mechanism: perspectives on recent research. Cell Mol Life Sci 61 (2004) 682-699
    • (2004) Cell Mol Life Sci , vol.61 , pp. 682-699
    • Jones, P.M.1    George, A.M.2
  • 3
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst P., and Elferink R.O. Mammalian ABC transporters in health and disease. Annu Rev Biochem 71 (2002) 537-592
    • (2002) Annu Rev Biochem , vol.71 , pp. 537-592
    • Borst, P.1    Elferink, R.O.2
  • 4
    • 34248594839 scopus 로고    scopus 로고
    • The emerging significance of the breast cancer resistance protein (ABCG2)
    • Hardwick L.J.A., Velamakanni S., and van Veen H.W. The emerging significance of the breast cancer resistance protein (ABCG2). Br J Pharmacol 151 (2007) 163-174
    • (2007) Br J Pharmacol , vol.151 , pp. 163-174
    • Hardwick, L.J.A.1    Velamakanni, S.2    van Veen, H.W.3
  • 6
    • 33947417310 scopus 로고    scopus 로고
    • Shedding light on drug transport: structure and function of the P-glycoprotein multidrug transporter (ABCB1)
    • Sharom F.J. Shedding light on drug transport: structure and function of the P-glycoprotein multidrug transporter (ABCB1). Biochem Cell Biol 84 (2006) 979-992
    • (2006) Biochem Cell Biol , vol.84 , pp. 979-992
    • Sharom, F.J.1
  • 7
    • 0029744881 scopus 로고    scopus 로고
    • Multidrug resistance mediated by a bacterial homologue of the human multidrug transporter MDR1
    • van Veen H.W., Venema K., Bolhuis H., Oussenko I., Kok J., Poolman B., et al. Multidrug resistance mediated by a bacterial homologue of the human multidrug transporter MDR1. Proc Natl Acad Sci USA 93 (1996) 10668-10672
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10668-10672
    • van Veen, H.W.1    Venema, K.2    Bolhuis, H.3    Oussenko, I.4    Kok, J.5    Poolman, B.6
  • 9
    • 33645836299 scopus 로고    scopus 로고
    • Lipid trafficking to the outer membrane of Gram-negative bacteria
    • Doerrler W.T. Lipid trafficking to the outer membrane of Gram-negative bacteria. Mol Microbiol 60 (2006) 542-552
    • (2006) Mol Microbiol , vol.60 , pp. 542-552
    • Doerrler, W.T.1
  • 10
    • 2942567775 scopus 로고    scopus 로고
    • Characterization of YvcC (BmrA), a multidrug ABC transporter constitutively expressed in Bacillus subtilis
    • Steinfels E., Orelle C., Fantino J.R., Dalmas O., Rigaud J.L., Denizot F., et al. Characterization of YvcC (BmrA), a multidrug ABC transporter constitutively expressed in Bacillus subtilis. Biochemistry 43 (2004) 7491-7502
    • (2004) Biochemistry , vol.43 , pp. 7491-7502
    • Steinfels, E.1    Orelle, C.2    Fantino, J.R.3    Dalmas, O.4    Rigaud, J.L.5    Denizot, F.6
  • 11
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson R.J., and Locher K.P. Structure of a bacterial multidrug ABC transporter. Nature 443 (2006) 180-185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 12
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson R.J., and Locher K.P. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett 581 (2007) 935-938
    • (2007) FEBS Lett , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 13
    • 0034212332 scopus 로고    scopus 로고
    • The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
    • Van Veen H.W., Margolles A., Muller M., Higgins C.F., and Konings W.N. The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism. EMBO J 19 (2000) 2503-2514
    • (2000) EMBO J , vol.19 , pp. 2503-2514
    • Van Veen, H.W.1    Margolles, A.2    Muller, M.3    Higgins, C.F.4    Konings, W.N.5
  • 14
    • 24944529951 scopus 로고    scopus 로고
    • A critical role of a carboxylate in proton conduction by the ATP-binding cassette multidrug transporter LmrA
    • Shilling R., Federici L., Walas F., Venter H., Velamakanni S., Woebking B., et al. A critical role of a carboxylate in proton conduction by the ATP-binding cassette multidrug transporter LmrA. FASEB J 19 (2005) 1698-1700
    • (2005) FASEB J , vol.19 , pp. 1698-1700
    • Shilling, R.1    Federici, L.2    Walas, F.3    Venter, H.4    Velamakanni, S.5    Woebking, B.6
  • 16
    • 0032518394 scopus 로고    scopus 로고
    • A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene
    • Van Veen H.W., Callaghan R., Soceneantu L., Sardini A., Konings W.N., and Higgins C.F. A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene. Nature 391 (1998) 291-295
    • (1998) Nature , vol.391 , pp. 291-295
    • Van Veen, H.W.1    Callaghan, R.2    Soceneantu, L.3    Sardini, A.4    Konings, W.N.5    Higgins, C.F.6
  • 17
    • 31844452870 scopus 로고    scopus 로고
    • The structures of MsbA: insight into ABC transporter-mediated multidrug efflux
    • Reyes C.L., Ward A., Yu J., and Chang G. The structures of MsbA: insight into ABC transporter-mediated multidrug efflux. FEBS Lett 580 (2006) 1042-1048
    • (2006) FEBS Lett , vol.580 , pp. 1042-1048
    • Reyes, C.L.1    Ward, A.2    Yu, J.3    Chang, G.4
  • 20
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 234 (1993) 779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 21
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., and Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J Mol Biol 231 (1993) 1049-1067
    • (1993) J Mol Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 22
    • 0030767485 scopus 로고    scopus 로고
    • Verify3D: assessment of protein models with three-dimensional profiles
    • Eisenberg D., Luthy R., and Bowie L.U. Verify3D: assessment of protein models with three-dimensional profiles. Methods Enzymol 277 (1997) 396-404
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, L.U.3
  • 23
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 24
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression for Lactococcus lactis with the food-grade inducer nisin
    • De Ruyter P.G., Kuipers O.P., and De Vos W.M. Controlled gene expression for Lactococcus lactis with the food-grade inducer nisin. Appl Environ Microbiol 62 (1996) 3662-3667
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3662-3667
    • De Ruyter, P.G.1    Kuipers, O.P.2    De Vos, W.M.3
  • 25
    • 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., and 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
  • 26
    • 0037052565 scopus 로고    scopus 로고
    • The Escherichia coli BtuCD structure: a framework for ABC transporter architecture and mechanism
    • Locher K.P., Lee A.T., and Rees D.C. The Escherichia 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
  • 27
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen J., Lu G., Lin J., Davidson A.L., and Quiocho F.A. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol Cell 12 (2003) 651-661
    • (2003) Mol Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 28
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., Thomas P.J., et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10 (2002) 139-149
    • (2002) Mol Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6
  • 29
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner K.P., Karcher A., Shin D.S., Craig L., Arthur L.M., Carney J.P., et al. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101 (2000) 789-800
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6
  • 30
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch of ABC transporters
    • Higgins C.F., and Linton K.J. The ATP switch of ABC transporters. Nat Struct Mol Biol 11 (2004) 918-926
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 31
    • 33846794508 scopus 로고    scopus 로고
    • About a switch: how P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work
    • Sauna Z.E., and Ambudkar S.V. About a switch: how P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work. Mol Cancer Ther 6 (2007) 13-23
    • (2007) Mol Cancer Ther , vol.6 , pp. 13-23
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 32
    • 0642272487 scopus 로고    scopus 로고
    • An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling
    • Stenham D.R., Campbell J.D., Sansom M.S., Higgins C.F., Kerr I.D., and Linton K.J. An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling. FASEB J 17 (2003) 2287-2289
    • (2003) FASEB J , vol.17 , pp. 2287-2289
    • Stenham, D.R.1    Campbell, J.D.2    Sansom, M.S.3    Higgins, C.F.4    Kerr, I.D.5    Linton, K.J.6
  • 33
    • 0042531543 scopus 로고    scopus 로고
    • A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure
    • Seigneuret M., and Garnier-Suillerot A. A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure. J Biol Chem 278 (2003) 30115-30124
    • (2003) J Biol Chem , vol.278 , pp. 30115-30124
    • Seigneuret, M.1    Garnier-Suillerot, A.2
  • 34
    • 13444266621 scopus 로고    scopus 로고
    • P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: a combined photo affinity labeling-protein homology modeling approach
    • Pleban K., Kopp S., Csaszar E., Peer M., Hrebicek T., Rizzi A., et al. P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: a combined photo affinity labeling-protein homology modeling approach. Mol Pharmacol 67 (2005) 365-374
    • (2005) Mol Pharmacol , vol.67 , pp. 365-374
    • Pleban, K.1    Kopp, S.2    Csaszar, E.3    Peer, M.4    Hrebicek, T.5    Rizzi, A.6
  • 35
    • 33646596002 scopus 로고    scopus 로고
    • The remarkable transport mechanism of P-glycoprotein: a multidrug transporter
    • Al-Shawi M.K., and Omote H. The remarkable transport mechanism of P-glycoprotein: a multidrug transporter. J Bioenerg Biomembr 37 (2005) 489-496
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 489-496
    • Al-Shawi, M.K.1    Omote, H.2
  • 36
    • 0347683446 scopus 로고    scopus 로고
    • Molecular modeling correctly predicts the functional importance of Phe594 in transmembrane helix 11 of the multidrug resistance protein. MRP1 (ABCC1)
    • Campbell J.D., Koike K., Moreau C., Sansom M.S., Deeley R.G., and Cole S.P. Molecular modeling correctly predicts the functional importance of Phe594 in transmembrane helix 11 of the multidrug resistance protein. MRP1 (ABCC1). J Biol Chem 279 (2004) 463-468
    • (2004) J Biol Chem , vol.279 , pp. 463-468
    • Campbell, J.D.1    Koike, K.2    Moreau, C.3    Sansom, M.S.4    Deeley, R.G.5    Cole, S.P.6
  • 37
    • 0037426344 scopus 로고    scopus 로고
    • Extending the structure of an ABC transporter to atomic resolution: modeling and simulation studies of MsbA
    • Campbell J.D., Biggin P.C., Baaden M., and Sansom M.S. Extending the structure of an ABC transporter to atomic resolution: modeling and simulation studies of MsbA. Biochemistry 42 (2003) 3666-3673
    • (2003) Biochemistry , vol.42 , pp. 3666-3673
    • Campbell, J.D.1    Biggin, P.C.2    Baaden, M.3    Sansom, M.S.4
  • 38
    • 27744528467 scopus 로고    scopus 로고
    • The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA
    • Dalmas O., Orelle C., Foucher A.E., Geourjon C., Crouzy S., Di Pietro A., et al. The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA. J Biol Chem 280 (2005) 36857-36864
    • (2005) J Biol Chem , vol.280 , pp. 36857-36864
    • Dalmas, O.1    Orelle, C.2    Foucher, A.E.3    Geourjon, C.4    Crouzy, S.5    Di Pietro, A.6
  • 39
    • 6944243952 scopus 로고    scopus 로고
    • A three-dimensional model for the substrate binding domain of the multidrug ATP binding cassette transporter LmrA
    • Ecker G.F., Pleban K., Kopp S., Csaszar E., Poelarends G.J., Putman M., et al. A three-dimensional model for the substrate binding domain of the multidrug ATP binding cassette transporter LmrA. Mol Pharmacol 66 (2004) 1169-1179
    • (2004) Mol Pharmacol , vol.66 , pp. 1169-1179
    • Ecker, G.F.1    Pleban, K.2    Kopp, S.3    Csaszar, E.4    Poelarends, G.J.5    Putman, M.6
  • 40
    • 1642565130 scopus 로고    scopus 로고
    • Reversible transport by the ATP-binding cassette multidrug export pump LmrA: ATP synthesis at the expense of downhill ethidium uptake
    • Balakrishnan L., Venter H., Shilling R.A., and Van Veen H.W. Reversible transport by the ATP-binding cassette multidrug export pump LmrA: ATP synthesis at the expense of downhill ethidium uptake. J Biol Chem 279 (2004) 11273-11280
    • (2004) J Biol Chem , vol.279 , pp. 11273-11280
    • Balakrishnan, L.1    Venter, H.2    Shilling, R.A.3    Van Veen, H.W.4


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