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Volumn 288, Issue 29, 2013, Pages 20785-20796

Association/dissociation of the nucleotide-binding domains of the atp-binding cassette protein MSBA measured during continuous hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ATP BINDING; ATP HYDROLYSIS; ATP-BINDING CASSETTE; CONTINUOUS HYDROLYSIS; MOLECULAR MECHANISM; NUCLEOTIDE-BINDING DOMAIN;

EID: 84880560706     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.477976     Document Type: Article
Times cited : (37)

References (41)
  • 1
    • 0036795485 scopus 로고    scopus 로고
    • Phylogenetic and functional classification of ATP-binding cassette (ABC) systems
    • Bouige, P., Laurent, D., Piloyan, L., and Dassa, E. (2002) Phylogenetic and functional classification of ATP-binding cassette (ABC) systems. Curr. Protein Pept. Sci. 3, 541-559
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 541-559
    • Bouige, P.1    Laurent, D.2    Piloyan, L.3    Dassa, E.4
  • 2
    • 84856305229 scopus 로고    scopus 로고
    • Catalytic and transport cycles of ABC exporters
    • Al-Shawi, M. K. (2011) Catalytic and transport cycles of ABC exporters. Essays Biochem. 50, 63-83
    • (2011) Essays Biochem. , vol.50 , pp. 63-83
    • Al-Shawi, M.K.1
  • 5
    • 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., and Hunt, J. F. (2002) ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10 139-149
    • (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    Hunt, J.F.7
  • 6
    • 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. (2003) A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12, 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
  • 7
    • 34147214716 scopus 로고    scopus 로고
    • Multiple molecular mechanisms for multidrug resistance transporters
    • Higgins, C. F. (2007) Multiple molecular mechanisms for multidrug resistance transporters. Nature 446, 749-757
    • (2007) Nature , vol.446 , pp. 749-757
    • Higgins, C.F.1
  • 8
    • 0038711772 scopus 로고    scopus 로고
    • The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p
    • Janas, E., Hofacker, M., Chen, M., Gompf, S., van der Does, C., and Tampe, R. (2003) The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J. Biol. Chem. 278,26862-26869
    • (2003) J. Biol. Chem. , vol.278 , pp. 26862-26869
    • Janas, E.1    Hofacker, M.2    Chen, M.3    Gompf, S.4    Van Der Does, C.5    Tampe, R.6
  • 10
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • Vergani, P., Lockless, S. W., Nairn, A. C., and Gadsby, D. C. (2005) CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 433, 876-880
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 12
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • Moody, J. E., Millen, L., Binns, D., Hunt, J. F., and Thomas, P. J. (2002) Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters. J. Biol. Chem. 277, 21111-21114
    • (2002) J. Biol. Chem. , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 14
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J., and Locher, K. P. (2006) Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 15
    • 34547943910 scopus 로고    scopus 로고
    • Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette. A computational study of the MJ0796 dimer
    • Jones, P. M., and George, A. M. (2007) Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette. A computational study of the MJ0796 dimer. J. Biol. Chem. 282, 22793-22803
    • (2007) J. Biol. Chem. , vol.282 , pp. 22793-22803
    • Jones, P.M.1    George, A.M.2
  • 16
    • 79960308124 scopus 로고    scopus 로고
    • Molecular-dynamics simulations of the ATP/apo state of a multidrug ATP-binding cassette transporter provide a structural and mechanistic basis for the asymmetric occluded state
    • Jones, P. M., and George, A. M. (2011) Molecular-dynamics simulations of the ATP/apo state of a multidrug ATP-binding cassette transporter provide a structural and mechanistic basis for the asymmetric occluded state. Biophys. J. 100, 3025-3034
    • (2011) Biophys. J. , vol.100 , pp. 3025-3034
    • Jones, P.M.1    George, A.M.2
  • 17
    • 36849067873 scopus 로고    scopus 로고
    • Catalytic cycle of ATP hydrolysis by P-glycoprotein. Evidence for formation of the E.S reaction intermediate with ATP 7S, a non-hydrolyzable analogue of ATP
    • Sauna, Z. E., Kim, I. W., Nandigama, K., Kopp, S., Chiba, P., and Ambud-kar, S. V. (2007) Catalytic cycle of ATP hydrolysis by P-glycoprotein. Evidence for formation of the E.S reaction intermediate with ATP7S, a non-hydrolyzable analogue of ATP. Biochemistry 46,13787-13799
    • (2007) Biochemistry , vol.46 , pp. 13787-13799
    • Sauna, Z.E.1    Kim, I.W.2    Nandigama, K.3    Kopp, S.4    Chiba, P.5    Ambud-Kar, S.V.6
  • 20
    • 18644362391 scopus 로고    scopus 로고
    • Structural basis ofenergy transduction in the transport cycle of MsbA
    • Dong, J., Yang, G., and McHaourab, H. S. (2005) Structural basis ofenergy transduction in the transport cycle of MsbA. Science 308, 1023-1028
    • (2005) Science , vol.308 , pp. 1023-1028
    • Dong, J.1    Yang, G.2    McHaourab, H.S.3
  • 21
    • 58849132410 scopus 로고    scopus 로고
    • Functionally important ATP binding and hydrolysis sites in Escherichia coli MsbA
    • Westfahl, K. M., Merten, J. A., Buchaklian, A. H., and Klug, C. S. (2008) Functionally important ATP binding and hydrolysis sites in Escherichia coli MsbA. Biochemistry47, 13878-13886
    • (2008) Biochemistry , vol.47 , pp. 13878-13886
    • Westfahl, K.M.1    Merten, J.A.2    Buchaklian, A.H.3    Klug, C.S.4
  • 23
    • 70349785154 scopus 로고    scopus 로고
    • Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA
    • Zou, P., and McHaourab, H. S. (2009) Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA. J. Mol. Biol. 393, 574-585
    • (2009) J. Mol. Biol. , vol.393 , pp. 574-585
    • Zou, P.1    McHaourab, H.S.2
  • 24
    • 0036085517 scopus 로고    scopus 로고
    • Principles and biophysical applications of lanthanide-based probes
    • Selvin, P. R. (2002) Principles and biophysical applications of lanthanide-based probes. Annu. Rev. Biophys. Biomol. Struct. 31, 275-302
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 275-302
    • Selvin, P.R.1
  • 25
    • 84860369537 scopus 로고    scopus 로고
    • Dissociation of ATP-binding cassette nucleotide-binding domain dimers into monomers during the hydrolysis cycle
    • Zoghbi, M. E., Krishnan, S., and Altenberg, G. A. (2012) Dissociation of ATP-binding cassette nucleotide-binding domain dimers into monomers during the hydrolysis cycle. J. Biol. Chem. 287, 14994-15000
    • (2012) J. Biol. Chem. , vol.287 , pp. 14994-15000
    • Zoghbi, M.E.1    Krishnan, S.2    Altenberg, G.A.3
  • 26
    • 84855476209 scopus 로고    scopus 로고
    • Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy
    • Verhalen, B., Ernst, S., Borsch, M., and Wilkens, S. (2012) Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy. J. Biol. Chem. 287, 1112-1127
    • (2012) J. Biol. Chem. , vol.287 , pp. 1112-1127
    • Verhalen, B.1    Ernst, S.2    Borsch, M.3    Wilkens, S.4
  • 29
    • 0037184103 scopus 로고    scopus 로고
    • ATPase activity of the MsbA lipid flippase of Escherichia coli
    • Doerrler, W. T., and Raetz, C. R. (2002) ATPase activity of the MsbA lipid flippase of Escherichia coli. J. Biol. Chem. 277, 36697-36705
    • (2002) J. Biol. Chem. , vol.277 , pp. 36697-36705
    • Doerrler, W.T.1    Raetz, C.R.2
  • 30
    • 84856733776 scopus 로고    scopus 로고
    • Kinetics of the association/dissociation cycle of an ATP-binding cassette nucleotide-binding domain
    • Zoghbi, M. E., Fuson, K. L., Sutton, R. B., and Altenberg, G. A. (2012) Kinetics of the association/dissociation cycle of an ATP-binding cassette nucleotide-binding domain. J. Biol. Chem. 287, 4157-4164
    • (2012) J. Biol. Chem. , vol.287 , pp. 4157-4164
    • Zoghbi, M.E.1    Fuson, K.L.2    Sutton, R.B.3    Altenberg, G.A.4
  • 32
    • 0033576580 scopus 로고    scopus 로고
    • Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
    • Cha, A., Snyder, G. E., Selvin, P. R., and Bezanilla, F. (1999) Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature 402, 809-813
    • (1999) Nature , vol.402 , pp. 809-813
    • Cha, A.1    Snyder, G.E.2    Selvin, P.R.3    Bezanilla, F.4
  • 33
    • 2342483844 scopus 로고    scopus 로고
    • Use of luminescence resonance energy transfer to measure distances in the AE1 anion exchange protein dimer
    • Knauf, P. A., and Pal, P. (2004) Use of luminescence resonance energy transfer to measure distances in the AE1 anion exchange protein dimer. Blood Cells Mol. Dis. 32, 360-365
    • (2004) Blood Cells Mol. Dis. , vol.32 , pp. 360-365
    • Knauf, P.A.1    Pal, P.2
  • 36
    • 79955750872 scopus 로고    scopus 로고
    • Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor
    • Rambhadran, A., Gonzalez, J., and Jayaraman, V. (2011) Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor. J. Biol. Chem. 286, 16953-16957
    • (2011) J. Biol. Chem. , vol.286 , pp. 16953-16957
    • Rambhadran, A.1    Gonzalez, J.2    Jayaraman, V.3
  • 38
    • 0029124166 scopus 로고
    • P-glyco-protein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch, I. L., Sankaran, B., Weber, J., and Senior, A. E. (1995) P-glyco-protein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J. Biol. Chem. 270,19383-19390
    • (1995) J. Biol. Chem. , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 39
    • 0033105255 scopus 로고    scopus 로고
    • Thiol-reactive luminescent chelates of terbium and europium
    • Chen, J., and Selvin, P. R. (1999) Thiol-reactive luminescent chelates of terbium and europium. Bioconjug. Chem. 10, 311-315
    • (1999) Bioconjug. Chem. , vol.10 , pp. 311-315
    • Chen, J.1    Selvin, P.R.2
  • 40
    • 0034822673 scopus 로고    scopus 로고
    • Quantum yields of luminescent lanthanide chelates and far-red dyes measured by resonance energy transfer
    • Xiao, M., and Selvin, P. R. (2001) Quantum yields of luminescent lanthanide chelates and far-red dyes measured by resonance energy transfer. J. Am. Chem. Soc. 123, 7067-7073
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7067-7073
    • Xiao, M.1    Selvin, P.R.2
  • 41
    • 0015918915 scopus 로고
    • Diffusion studies of phosphatydilcholine vesicles
    • Huang, C., and Lee, L. (1973) Diffusion studies of phosphatydilcholine vesicles. J. Am. Chem. Soc. 95, 234-239
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 234-239
    • Huang, C.1    Lee, L.2


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