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Volumn 6, Issue 4, 2010, Pages

Asymmetric switching in a homodimeric ABC transporter: A simulation study

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BIOLOGICAL MEMBRANES; COMPUTER ARCHITECTURE; CRYSTAL STRUCTURE; DIMERS; ION EXCHANGE; MOLECULAR DYNAMICS; NUCLEOTIDES; PROTEINS;

EID: 77954613193     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000762     Document Type: Article
Times cited : (68)

References (50)
  • 2
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • Gadsby DC, Vergani P, Csanády L (2006) The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature 440: 477-483.
    • (2006) Nature , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanády, L.3
  • 3
    • 61449361477 scopus 로고    scopus 로고
    • Review. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator
    • Muallem D, Vergani P (2009) Review. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator. Philos Trans R Soc B Biol Sci 364: 247-55.
    • (2009) Philos Trans R Soc B Biol Sci , vol.364 , pp. 247-255
    • Muallem, D.1    Vergani, P.2
  • 4
    • 33846658399 scopus 로고    scopus 로고
    • ABCC8 and ABCC9: ABC transporters that regulate K+ channels
    • Bryan J, Muñoz A, Zhang X, Düfer M, Drews G, et al. (2007) ABCC8 and ABCC9: ABC transporters that regulate K+ channels. Pflugers Arch 453: 703-18.
    • (2007) Pflugers Arch , vol.453 , pp. 703-718
    • Bryan, J.1    Muñoz, A.2    Zhang, X.3    Düfer, M.4    Drews, G.5
  • 5
    • 61449365340 scopus 로고    scopus 로고
    • Review. SUR1: A unique ATP-binding cassette protein that functions as an ion channel regulator
    • Aittoniemi J, Fotinou C, Craig TJ, de Wet H, Proks P, et al. (2009) Review. SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator. Philos Trans R Soc B Biol Sci 364: 257-67.
    • (2009) Philos Trans R Soc B Biol Sci , vol.364 , pp. 257-267
    • Aittoniemi, J.1    Fotinou, C.2    Craig, T.J.3    de Wet, H.4    Proks, P.5
  • 8
    • 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 AL, Quiocho FA (2003) A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol Cell 12: 651-61.
    • (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
  • 11
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABCATPase domain dimer
    • Zaitseva J, Oswald C, Jumpertz T, Jenewein S, Wiedenmann A, et al. (2006) A structural analysis of asymmetry required for catalytic activity of an ABCATPase domain dimer. EMBO J 25: 3432-43.
    • (2006) EMBO J , vol.25 , pp. 3432-3443
    • Zaitseva, J.1    Oswald, C.2    Jumpertz, T.3    Jenewein, S.4    Wiedenmann, A.5
  • 12
    • 44349100345 scopus 로고    scopus 로고
    • Functionally important interactions between the nucleotide-binding domains of an antigenic peptide transporter
    • Procko E, Gaudet R (2008) Functionally important interactions between the nucleotide-binding domains of an antigenic peptide transporter. Biochemistry 47: 5699-708.
    • (2008) Biochemistry , vol.47 , pp. 5699-5708
    • Procko, E.1    Gaudet, R.2
  • 13
    • 0033816117 scopus 로고    scopus 로고
    • ATPase activity of the sulfonylurea receptor: A catalytic function for the KATP channel complex
    • Bienengraeber M, Alekseev AE, Abraham MR, Carrasco AJ, Moreau C, et al. (2000) ATPase activity of the sulfonylurea receptor: a catalytic function for the KATP channel complex. FASEB J 14: 1943-1952.
    • (2000) FASEB J , vol.14 , pp. 1943-1952
    • Bienengraeber, M.1    Alekseev, A.E.2    Abraham, M.R.3    Carrasco, A.J.4    Moreau, C.5
  • 14
    • 4744343547 scopus 로고    scopus 로고
    • A heteromeric complex of the two nucleotide binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) mediates ATPase activity
    • Kidd JF, Ramjeesingh M, Stratford F, Huan L, Bear CE (2004) A heteromeric complex of the two nucleotide binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) mediates ATPase activity. J Biol Chem 279: 41664-41669.
    • (2004) J Biol Chem , vol.279 , pp. 41664-41669
    • Kidd, J.F.1    Ramjeesingh, M.2    Stratford, F.3    Huan, L.4    Bear, C.E.5
  • 15
  • 16
    • 44949120657 scopus 로고    scopus 로고
    • Investigating the role of the invariant carboxylate residues E552 and E1197 in the catalytic activity of ABCB1a (mouse MDR3)
    • Carrier I, Gros P (2008) Investigating the role of the invariant carboxylate residues E552 and E1197 in the catalytic activity of ABCB1a (mouse MDR3). FEBS J 275: 3312-24.
    • (2008) FEBS J , vol.275 , pp. 3312-3324
    • Carrier, I.1    Gros, P.2
  • 17
    • 33749076230 scopus 로고    scopus 로고
    • Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter
    • Procko E, Ferrin-O'Connell I, Ng S, Gaudet R (2006) Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter. Mol Cell 24: 51-62.
    • (2006) Mol Cell , vol.24 , pp. 51-62
    • Procko, E.1    Ferrin-O'Connell, I.2    Ng, S.3    Gaudet, R.4
  • 18
    • 70349333637 scopus 로고    scopus 로고
    • The mechanism of ABC transporters: General lessons from structural and functional studies of an antigenic peptide transporter
    • Procko E, O'Mara ML, Bennett WFD, Tieleman DP, Gaudet R (2009) The mechanism of ABC transporters: general lessons from structural and functional studies of an antigenic peptide transporter. FASEB J 23: 1287-1302.
    • (2009) FASEB J , vol.23 , pp. 1287-1302
    • Procko, E.1    O'Mara, M.L.2    Bennett, W.F.D.3    Tieleman, D.P.4    Gaudet, R.5
  • 19
    • 33745835398 scopus 로고    scopus 로고
    • Transmembrane transport of endoand xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins
    • Deeley RG, Westlake C, Cole SPC (2006) Transmembrane transport of endoand xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. Physiol Rev 86: 849-99.
    • (2006) Physiol Rev , vol.86 , pp. 849-899
    • Deeley, R.G.1    Westlake, C.2    Cole, S.P.C.3
  • 20
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson RJP, Locher KP (2006) Structure of a bacterial multidrug ABC transporter. Nature 443: 180-5.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 21
    • 50849114847 scopus 로고    scopus 로고
    • Multidrug transport by the ABC transporter Sav1866 from Staphylococcus aureus
    • Velamakanni S, Yao Y, Gutmann DAP, van Veen HW (2008) Multidrug transport by the ABC transporter Sav1866 from Staphylococcus aureus. Biochemistry 47: 9300-8.
    • (2008) Biochemistry , vol.47 , pp. 9300-9308
    • Velamakanni, S.1    Yao, Y.2    Gutmann, D.A.P.3    van Veen, H.W.4
  • 22
    • 36849079744 scopus 로고    scopus 로고
    • Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein
    • Zolnerciks JK, Wooding C, Linton KJ (2007) Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein. FASEB J 21: 3937-48.
    • (2007) FASEB J , vol.21 , pp. 3937-3948
    • Zolnerciks, J.K.1    Wooding, C.2    Linton, K.J.3
  • 23
    • 38349016587 scopus 로고    scopus 로고
    • Structure-based interpretation of the mutagenesis database for the nucleotide binding domains of P-glycoprotein
    • Lawson J, O'Mara ML, Kerr ID (2008) Structure-based interpretation of the mutagenesis database for the nucleotide binding domains of P-glycoprotein. Biochim Biophys Acta 1778: 376-91.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 376-391
    • Lawson, J.1    O'Mara, M.L.2    Kerr, I.D.3
  • 24
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • Serohijos AWR, Hegedus T, Aleksandrov AA, He L, Cui L, et al. (2008) Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function. Proc Natl Acad Sci USA 105: 3256-61.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3256-3261
    • Serohijos, A.W.R.1    Hegedus, T.2    Aleksandrov, A.A.3    He, L.4    Cui, L.5
  • 25
    • 34147168584 scopus 로고    scopus 로고
    • Simulation of the coupling between nucleotide binding and transmembrane domains in the ATP binding cassette transporter BtuCD
    • Sonne J, Kandt C, Peters GH, Hansen FY, Jensen MØ, et al. (2007) Simulation of the coupling between nucleotide binding and transmembrane domains in the ATP binding cassette transporter BtuCD. Biophys J 92: 2727-2734.
    • (2007) Biophys J , vol.92 , pp. 2727-2734
    • Sonne, J.1    Kandt, C.2    Peters, G.H.3    Hansen, F.Y.4    Jensen, M.Ø.5
  • 26
    • 33947284958 scopus 로고    scopus 로고
    • Dynamics and function in a bacterial ABC transporter: Simulation studies of the BtuCDF system and its components
    • Ivetac A, Campbell JD, Sansom MSP (2007) Dynamics and function in a bacterial ABC transporter: simulation studies of the BtuCDF system and its components. Biochemistry 46: 2767-2778.
    • (2007) Biochemistry , vol.46 , pp. 2767-2778
    • Ivetac, A.1    Campbell, J.D.2    Sansom, M.S.P.3
  • 27
    • 33748776270 scopus 로고    scopus 로고
    • The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter
    • Oloo EO, Fung EY, Tieleman DP (2006) The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter. J Biol Chem 281: 28397-407.
    • (2006) J Biol Chem , vol.281 , pp. 28397-28407
    • Oloo, E.O.1    Fung, E.Y.2    Tieleman, D.P.3
  • 28
    • 0036789902 scopus 로고    scopus 로고
    • Mechanism of ABC transporters: A molecular dynamics simulation of a well characterized nucleotide-binding subunit
    • Jones PM, George AM (2002) Mechanism of ABC transporters: a molecular dynamics simulation of a well characterized nucleotide-binding subunit. Proc Nat Acad Sci USA 99: 12639-12644.
    • (2002) Proc Nat Acad Sci USA , vol.99 , pp. 12639-12644
    • Jones, P.M.1    George, A.M.2
  • 29
    • 7244240754 scopus 로고    scopus 로고
    • Conformational transitions induced by the binding of MgATP to the vitamin B12 ATP-binding cassette (ABC) transporter BtuCD
    • Oloo EO, Tieleman DP (2004) Conformational transitions induced by the binding of MgATP to the vitamin B12 ATP-binding cassette (ABC) transporter BtuCD. J Biol Chem 279: 45013-9.
    • (2004) J Biol Chem , vol.279 , pp. 45013-45019
    • Oloo, E.O.1    Tieleman, D.P.2
  • 30
    • 34547943910 scopus 로고    scopus 로고
    • Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: A computational study of the MJ0796 dimer
    • Jones PM, George AM (2007) Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: a computational study of the MJ0796 dimer. J Biol Chem 282: 22793-803.
    • (2007) J Biol Chem , vol.282 , pp. 22793-22803
    • Jones, P.M.1    George, A.M.2
  • 31
    • 66149139241 scopus 로고    scopus 로고
    • Opening of the ADP-bound active site in the ABC transporter ATPase dimer: Evidence for a constant contact, alternating sites model for the catalytic cycle
    • Jones PM, George AM (2009) Opening of the ADP-bound active site in the ABC transporter ATPase dimer: evidence for a constant contact, alternating sites model for the catalytic cycle. Proteins 75: 387-396.
    • (2009) Proteins , vol.75 , pp. 387-396
    • Jones, P.M.1    George, A.M.2
  • 32
    • 58149359858 scopus 로고    scopus 로고
    • Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis
    • Wen P, Tajkhorshid E (2008) Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis. Biophys J 95: 5100-5110.
    • (2008) Biophys J , vol.95 , pp. 5100-5110
    • Wen, P.1    Tajkhorshid, E.2
  • 33
    • 4143116650 scopus 로고    scopus 로고
    • Computational studies of membrane channels
    • Roux B, Schulten K (2004) Computational studies of membrane channels. Structure 12: 1343-1351.
    • (2004) Structure , vol.12 , pp. 1343-1351
    • Roux, B.1    Schulten, K.2
  • 36
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen HJC, van der Spoel D, van Drunen R (1995) GROMACS: A message-passing parallel molecular dynamics implementation. Comp Phys Comm 91: 43-56.
    • (1995) Comp Phys Comm , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    van der Spoel, D.2    van Drunen, R.3
  • 37
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Mod 7: 306-317.
    • (2001) J Mol Mod , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 39
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink C, Villa A, Mark AE, Gunsteren WFV (2004) A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6. J Comp Chem 25: 1656-1676.
    • (2004) J Comp Chem , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Gunsteren, W.F.V.4
  • 41
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An N log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 44
    • 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, Karcher A, Shin DS, Craig L, Arthur LM, et al. (2000) Structural Biology of Rad50 ATPase: ATP-Driven Conformational Control in DNA Double-Strand Break Repair and the ABC-ATPase Superfamily. Cell 101: 789-800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5
  • 45
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith PC, Karpowich N, Millen L, Moody JE, Rosen J, et al. (2002) ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10: 139-49.
    • (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
  • 46
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva J, Jenewein S, Jumpertz T, Holland IB, Schmitt L (2005) H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J 24: 1901-10.
    • (2005) EMBO J , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 47
    • 57649183334 scopus 로고    scopus 로고
    • Functional clustering of mutations in the dimmer interface of the nucleotide binding folds of the sulfonylurea receptor
    • Masia R, Nichols CG (2008) Functional clustering of mutations in the dimmer interface of the nucleotide binding folds of the sulfonylurea receptor. J Biol Chem 283: 30322-9.
    • (2008) J Biol Chem , vol.283 , pp. 30322-30329
    • Masia, R.1    Nichols, C.G.2
  • 48
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson RJP, Locher KP (2007) Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett 581: 935-8.
    • (2007) FEBS Lett , vol.581 , pp. 935-938
    • Dawson, R.J.P.1    Locher, K.P.2
  • 50
    • 63449139456 scopus 로고    scopus 로고
    • Structure of Pglycoprotein reveals a molecular basis for poly-specific drug binding
    • Aller SG, Yu J, Ward A, Weng Y, Chittaboina S, et al. (2009) Structure of Pglycoprotein reveals a molecular basis for poly-specific drug binding. Science 323: 1718-1722.
    • (2009) Science , vol.323 , pp. 1718-1722
    • Aller, S.G.1    Yu, J.2    Ward, A.3    Weng, Y.4    Chittaboina, S.5


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