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Volumn 5, Issue JANUARY2016, 2016, Pages

Revealing an outward-facing open conformational state in a CLC CL-/H+ exchange transporter

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE CHANNEL PROTON CHLORIDE EXCHANGE TRANSPORTER; MEMBRANE PROTEIN; TEMPOL; UNCLASSIFIED DRUG; CHLORIDE CHANNEL; CLC PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN;

EID: 84979547129     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.11189     Document Type: Article
Times cited : (38)

References (113)
  • 2
    • 33748798473 scopus 로고    scopus 로고
    • Synergism between halide binding and proton transport in a CLC-type exchanger
    • Accardi A, Lobet S, Williams C, Miller C, Dutzler R. 2006. Synergism between halide binding and proton transport in a CLC-type exchanger. Journal of Molecular Biology 362:691-699. doi: 10.1016/j.jmb.2006.07.081
    • (2006) Journal of Molecular Biology , vol.362 , pp. 691-699
    • Accardi, A.1    Lobet, S.2    Williams, C.3    Miller, C.4    Dutzler, R.5
  • 3
    • 1542288949 scopus 로고    scopus 로고
    • Secondary active transport mediated by a prokaryotic homologue of ClC cl- channels
    • Accardi A, Miller C. 2004. Secondary active transport mediated by a prokaryotic homologue of ClC cl- channels. Nature 427:803-807. doi: 10.1038/nature02314
    • (2004) Nature , vol.427 , pp. 803-807
    • Accardi, A.1    Miller, C.2
  • 4
    • 77953808359 scopus 로고    scopus 로고
    • CLC channels and transporters: Proteins with borderline personalities
    • Accardi A, Picollo A. 2010. CLC channels and transporters: proteins with borderline personalities. Biochimica Et Biophysica Acta 1798:1457-1464. doi: 10.1016/j.bbamem.2010.02.022
    • (2010) Biochimica Et Biophysica Acta , vol.1798 , pp. 1457-1464
    • Accardi, A.1    Picollo, A.2
  • 6
    • 84941584554 scopus 로고    scopus 로고
    • Structure and gating of CLC channels and exchangers
    • Accardi A. 2015. Structure and gating of CLC channels and exchangers. The Journal of Physiology 593:4129-4138. doi: 10.1113/JP270575
    • (2015) The Journal of Physiology , vol.593 , pp. 4129-4138
    • Accardi, A.1
  • 7
    • 58149213832 scopus 로고    scopus 로고
    • Structural analysis of ion selectivity in the NaK channel
    • Alam A, Jiang Y. 2009. Structural analysis of ion selectivity in the NaK channel. Nature Structural & Molecular Biology 16:35-41. doi: 10.1038/nsmb.1537
    • (2009) Nature Structural & Molecular Biology , vol.16 , pp. 35-41
    • Alam, A.1    Jiang, Y.2
  • 8
    • 0027441950 scopus 로고
    • Essential dynamics of proteins
    • Amadei A, Linssen AB, Berendsen HJ. 1993. Essential dynamics of proteins. Proteins 17:412-425. doi: 10.1002/prot.340170408
    • (1993) Proteins , vol.17 , pp. 412-425
    • Amadei, A.1    Linssen, A.B.2    Berendsen, H.J.3
  • 9
    • 77949634796 scopus 로고    scopus 로고
    • Normal mode analysis of biomolecular structures: Functional mechanisms of membrane proteins
    • Bahar I, Lezon TR, Bakan A, Shrivastava IH. 2010. Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins. Chemical Reviews 110:1463-1497. doi: 10.1021/cr900095e
    • (2010) Chemical Reviews , vol.110 , pp. 1463-1497
    • Bahar, I.1    Lezon, T.R.2    Bakan, A.3    Shrivastava, I.H.4
  • 10
    • 84941254171 scopus 로고    scopus 로고
    • A proteoliposome-based efflux assay to determine single-molecule properties of cl-channels and transporters
    • Basilio D, Accardi A. 2015. A proteoliposome-based efflux assay to determine single-molecule properties of cl-channels and transporters. Journal of Visualized Experiments. doi: 10.3791/52369
    • (2015) Journal of Visualized Experiments
    • Basilio, D.1    Accardi, A.2
  • 11
    • 84902107617 scopus 로고    scopus 로고
    • Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter
    • Basilio D, Noack K, Picollo A, Accardi A. 2014. Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter. Nature Structural & Molecular Biology 21:456-463. doi: 10.1038/nsmb.2814
    • (2014) Nature Structural & Molecular Biology , vol.21 , pp. 456-463
    • Basilio, D.1    Noack, K.2    Picollo, A.3    Accardi, A.4
  • 12
    • 33744950592 scopus 로고    scopus 로고
    • Site-directed fluorescence studies of a prokaryotic ClC antiporter
    • Bell SP, Curran PK, Choi S, Mindell JA. 2006. Site-directed fluorescence studies of a prokaryotic ClC antiporter. Biochemistry 45:6773-6782. doi: 10.1021/bi0523815
    • (2006) Biochemistry , vol.45 , pp. 6773-6782
    • Bell, S.P.1    Curran, P.K.2    Choi, S.3    Mindell, J.A.4
  • 14
    • 4444366193 scopus 로고    scopus 로고
    • Exterior site occupancy infers chloride-induced proton gating in a prokaryotic homolog of the ClC chloride channel
    • Bostick DL, Berkowitz ML. 2004. Exterior site occupancy infers chloride-induced proton gating in a prokaryotic homolog of the ClC chloride channel. Biophysical Journal 87:1686-1696. doi: 10.1529/biophysj.104.042465
    • (2004) Biophysical Journal , vol.87 , pp. 1686-1696
    • Bostick, D.L.1    Berkowitz, M.L.2
  • 16
    • 46249093730 scopus 로고    scopus 로고
    • Influence of the chloride channel of fusarium oxysporum on extracellular laccase activity and virulence on tomato plants
    • Cañero DC, Roncero MI. 2008. Influence of the chloride channel of fusarium oxysporum on extracellular laccase activity and virulence on tomato plants. Microbiology 154:1474-1481. doi: 10.1099/mic.0.2007/015388-0
    • (2008) Microbiology , vol.154 , pp. 1474-1481
    • Cañero, D.C.1    Roncero, M.I.2
  • 17
    • 15544388091 scopus 로고    scopus 로고
    • Structure and function of clc channels
    • Chen TY. 2005. Structure and function of clc channels. Annual Review of Physiology 67:809-839. doi: 10.1146/annurev.physiol.67.032003.153012
    • (2005) Annual Review of Physiology , vol.67 , pp. 809-839
    • Chen, T.Y.1
  • 18
    • 84858758947 scopus 로고    scopus 로고
    • Molecular dynamics investigation of cl- and water transport through a eukaryotic CLC transporter
    • Cheng MH, Coalson RD. 2012. Molecular dynamics investigation of cl- and water transport through a eukaryotic CLC transporter. Biophysical Journal 102:1363-1371. doi: 10.1016/j.bpj.2012.01.056
    • (2012) Biophysical Journal , vol.102 , pp. 1363-1371
    • Cheng, M.H.1    Coalson, R.D.2
  • 19
    • 1142291714 scopus 로고    scopus 로고
    • Mechanism of anionic conduction across ClC
    • Cohen J, Schulten K. 2004. Mechanism of anionic conduction across ClC. Biophysical Journal 86:836-845. doi: 10.1016/S0006-3495(04)74159-4
    • (2004) Biophysical Journal , vol.86 , pp. 836-845
    • Cohen, J.1    Schulten, K.2
  • 21
    • 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. The Journal of Chemical Physics 98:10089-10092. doi: 10.1063/1.464397
    • (1993) The Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 22
    • 84941600343 scopus 로고    scopus 로고
    • Chloride transporters and receptor-mediated endocytosis in the renal proximal tubule
    • Devuyst O, Luciani A. 2015. Chloride transporters and receptor-mediated endocytosis in the renal proximal tubule. The Journal of Physiology 593:4151-4164. doi: 10.1113/JP270087
    • (2015) The Journal of Physiology , vol.593 , pp. 4151-4164
    • Devuyst, O.1    Luciani, A.2
  • 23
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 A ° reveals the molecular basis of anion selectivity
    • Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R. 2002. X-ray structure of a ClC chloride channel at 3.0 A ° reveals the molecular basis of anion selectivity. Nature 415:287-294. doi: 10.1038/415287a
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 24
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler R, Campbell EB, MacKinnon R. 2003. Gating the selectivity filter in ClC chloride channels. Science 300: 108-112. doi: 10.1126/science.1082708
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 25
    • 34249881600 scopus 로고    scopus 로고
    • A structural perspective on ClC channel and transporter function
    • Dutzler R. 2007. A structural perspective on ClC channel and transporter function. FEBS Letters 581:2839-2844. doi: 10.1016/j.febslet.2007.04.016
    • (2007) FEBS Letters , vol.581 , pp. 2839-2844
    • Dutzler, R.1
  • 26
    • 70350304561 scopus 로고    scopus 로고
    • Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR
    • Elvington SM, Liu CW, Maduke MC. 2009. Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR. The EMBO Journal 28:3090-3102. doi: 10.1038/emboj.2009.259
    • (2009) The EMBO Journal , vol.28 , pp. 3090-3102
    • Elvington, S.M.1    Liu, C.W.2    Maduke, M.C.3
  • 27
    • 70049114997 scopus 로고    scopus 로고
    • Thinking outside the crystal: Complementary approaches for examining transporter mechanism
    • Elvington SM, Maduke M. 2008. Thinking outside the crystal: complementary approaches for examining transporter mechanism. Channels 2:373-379. doi: 10.4161/chan.2.5.6903
    • (2008) Channels , vol.2 , pp. 373-379
    • Elvington, S.M.1    Maduke, M.2
  • 29
    • 84875675509 scopus 로고    scopus 로고
    • Connecting protein conformational dynamics with catalytic function as illustrated in dihydrofolate reductase
    • Fan Y, Cembran A, Ma S, Gao J. 2013. Connecting protein conformational dynamics with catalytic function as illustrated in dihydrofolate reductase. Biochemistry 52:2036-2049. doi: 10.1021/bi301559q
    • (2013) Biochemistry , vol.52 , pp. 2036-2049
    • Fan, Y.1    Cembran, A.2    Ma, S.3    Gao, J.4
  • 30
    • 2542437774 scopus 로고    scopus 로고
    • Electrostatics of ion stabilization in a ClC chloride channel homologue from escherichia coli
    • Faraldo-Gómez JD, Roux B. 2004. Electrostatics of ion stabilization in a ClC chloride channel homologue from escherichia coli. Journal of Molecular Biology 339:981-1000. doi: 10.1016/j.jmb.2004.04.023
    • (2004) Journal of Molecular Biology , vol.339 , pp. 981-1000
    • Faraldo-Gómez, J.D.1    Roux, B.2
  • 31
    • 78049362741 scopus 로고    scopus 로고
    • Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle
    • Feng L, Campbell EB, Hsiung Y, MacKinnon R. 2010. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330:635-641. doi: 10.1126/science.1195230
    • (2010) Science , vol.330 , pp. 635-641
    • Feng, L.1    Campbell, E.B.2    Hsiung, Y.3    MacKinnon, R.4
  • 33
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • Forrest LR, Krämer R, Ziegler C. 2011. The structural basis of secondary active transport mechanisms. Biochimica Et Biophysica Acta 1807:167-188. doi: 10.1016/j.bbabio.2010.10.014
    • (2011) Biochimica Et Biophysica Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Krämer, R.2    Ziegler, C.3
  • 37
    • 84885458692 scopus 로고    scopus 로고
    • Global motions exhibited by proteins in micro- to milliseconds simulations concur with anisotropic network model predictions
    • Gur M, Zomot E, Bahar I. 2013. Global motions exhibited by proteins in micro- to milliseconds simulations concur with anisotropic network model predictions. The Journal of Chemical Physics 139:121912. doi: 10.1063/1.4816375
    • (2013) The Journal of Chemical Physics , vol.139 , pp. 121912
    • Gur, M.1    Zomot, E.2    Bahar, I.3
  • 39
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover WG. 1985. Canonical dynamics: equilibrium phase-space distributions. Physical Review A 31:1695-1697. doi: 10.1103/PhysRevA.31.1695
    • (1985) Physical Review A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 42
    • 47749099638 scopus 로고    scopus 로고
    • Mechanism of signal propagation upon retinal isomerization: Insights from molecular dynamics simulations of rhodopsin restrained by normal modes
    • Isin B, Schulten K, Tajkhorshid E, Bahar I. 2008. Mechanism of signal propagation upon retinal isomerization: insights from molecular dynamics simulations of rhodopsin restrained by normal modes. Biophysical Journal 95: 789-803. doi: 10.1529/biophysj.107.120691
    • (2008) Biophysical Journal , vol.95 , pp. 789-803
    • Isin, B.1    Schulten, K.2    Tajkhorshid, E.3    Bahar, I.4
  • 43
    • 84934442060 scopus 로고    scopus 로고
    • Identification of motions in membrane proteins by elastic network models and their experimental validation
    • Isin B, Tirupula KC, Oltvai ZN, Klein-Seetharaman J, Bahar I. 2012. Identification of motions in membrane proteins by elastic network models and their experimental validation. Methods in Molecular Biology 914:285-317. doi: 10.1007/978-1-62703-023-6_17
    • (2012) Methods in Molecular Biology , vol.914 , pp. 285-317
    • Isin, B.1    Tirupula, K.C.2    Oltvai, Z.N.3    Klein-Seetharaman, J.4    Bahar, I.5
  • 44
    • 0037126294 scopus 로고    scopus 로고
    • A biological role for prokaryotic ClC chloride channels
    • Iyer R, Iverson TM, Accardi A, Miller C. 2002. A biological role for prokaryotic ClC chloride channels. Nature 419: 715-718. doi: 10.1038/nature01000
    • (2002) Nature , vol.419 , pp. 715-718
    • Iyer, R.1    Iverson, T.M.2    Accardi, A.3    Miller, C.4
  • 45
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O. 1966. Simple allosteric model for membrane pumps. Nature 211:969-970. doi: 10.1038/211969a0
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 47
    • 79952074056 scopus 로고    scopus 로고
    • Structure of a slow CLC Cl/H+ antiporter from a cyanobacterium
    • Jayaram H, Robertson JL, Wu F, Williams C, Miller C. 2011. Structure of a slow CLC Cl/H+ antiporter from a cyanobacterium. Biochemistry 50:788-794. doi: 10.1021/bi1019258
    • (2011) Biochemistry , vol.50 , pp. 788-794
    • Jayaram, H.1    Robertson, J.L.2    Wu, F.3    Williams, C.4    Miller, C.5
  • 48
    • 39849092445 scopus 로고    scopus 로고
    • CLC chloride channels and transporters: From genes to protein structure, pathology and physiology
    • Jentsch TJ. 2008. CLC chloride channels and transporters: from genes to protein structure, pathology and physiology. Critical Reviews in Biochemistry and Molecular Biology 43:3-36. doi: 10.1080/10409230701829110
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , pp. 3-36
    • Jentsch, T.J.1
  • 49
    • 84941570211 scopus 로고    scopus 로고
    • Discovery of CLC transport proteins: Cloning, structure, function and pathophysiology
    • Jentsch TJ. 2015. Discovery of CLC transport proteins: cloning, structure, function and pathophysiology. The Journal of Physiology 593:4091-4109. doi: 10.1113/JP270043
    • (2015) The Journal of Physiology , vol.593 , pp. 4091-4109
    • Jentsch, T.J.1
  • 50
    • 84859888767 scopus 로고    scopus 로고
    • DEER distance measurements on proteins
    • Jeschke G. 2012. DEER distance measurements on proteins. Annual Review of Physical Chemistry 63:419-446. doi: 10.1146/annurev-physchem-032511-143716
    • (2012) Annual Review of Physical Chemistry , vol.63 , pp. 419-446
    • Jeschke, G.1
  • 53
    • 76449099287 scopus 로고    scopus 로고
    • XDS. Acta Crystallographica
    • Section D
    • Kabsch W. 2010. XDS. Acta Crystallographica. Section D, Biological Crystallography 66:125-132. doi: 10.1107/S0907444909047337
    • (2010) Biological Crystallography , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 56
    • 84865396279 scopus 로고    scopus 로고
    • Partial least-squares functional mode analysis: Application to the membrane proteins AQP1, Aqy1, and CLC-ec1
    • Krivobokova T, Briones R, Hub JS, Munk A, de Groot BL. 2012. Partial least-squares functional mode analysis: application to the membrane proteins AQP1, Aqy1, and CLC-ec1. Biophysical Journal 103:786-796. doi: 10.1016/j.bpj.2012.07.022
    • (2012) Biophysical Journal , vol.103 , pp. 786-796
    • Krivobokova, T.1    Briones, R.2    Hub, J.S.3    Munk, A.4    de Groot, B.L.5
  • 57
    • 34249897242 scopus 로고    scopus 로고
    • Proton pathways and h+/Cl- stoichiometry in bacterial chloride transporters
    • Kuang Z, Mahankali U, Beck TL. 2007. Proton pathways and h+/Cl- stoichiometry in bacterial chloride transporters. Proteins 68:26-33. doi: 10.1002/prot.21441
    • (2007) Proteins , vol.68 , pp. 26-33
    • Kuang, Z.1    Mahankali, U.2    Beck, T.L.3
  • 59
    • 79957896458 scopus 로고    scopus 로고
    • ClC-7 is a slowly voltage-gated 2Cl(-)/1H(+)-exchanger and requires Ostm1 for transport activity
    • Leisle L, Ludwig CF, Wagner FA, Jentsch TJ, Stauber T. 2011. ClC-7 is a slowly voltage-gated 2Cl(-)/1H(+)-exchanger and requires Ostm1 for transport activity. The EMBO Journal 30:2140-2152. doi: 10.1038/emboj.2011.137
    • (2011) The EMBO Journal , vol.30 , pp. 2140-2152
    • Leisle, L.1    Ludwig, C.F.2    Wagner, F.A.3    Jentsch, T.J.4    Stauber, T.5
  • 61
    • 62349093404 scopus 로고    scopus 로고
    • Intracellular proton-transfer mutants in a CLC cl-/H+ exchanger
    • Lim HH, Miller C. 2009. Intracellular proton-transfer mutants in a CLC cl-/H+ exchanger. The Journal of General Physiology 133:131-138. doi: 10.1085/jgp.200810112
    • (2009) The Journal of General Physiology , vol.133 , pp. 131-138
    • Lim, H.H.1    Miller, C.2
  • 62
    • 84871701543 scopus 로고    scopus 로고
    • Intracellular proton access in a cl(-)/H(+) antiporter
    • Lim HH, Shane T, Miller C. 2012. Intracellular proton access in a cl(-)/H(+) antiporter. PLoS Biology 10:e1001441. doi: 10.1371/journal.pbio.1001441
    • (2012) PLoS Biology , vol.10
    • Lim, H.H.1    Shane, T.2    Miller, C.3
  • 64
    • 33746565283 scopus 로고    scopus 로고
    • Molecular dynamics of apo-adenylate kinase: A principal component analysis
    • Lou H, Cukier RI. 2006. Molecular dynamics of apo-adenylate kinase: a principal component analysis. The Journal of Physical Chemistry. B 110:12796-12808. doi: 10.1021/jp061976m
    • (2006) The Journal of Physical Chemistry. B , vol.110 , pp. 12796-12808
    • Lou, H.1    Cukier, R.I.2
  • 65
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell AD, Feig M, Brooks CL. 2004. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. Journal of Computational Chemistry 25:1400-1415. doi: 10.1002/jcc.20065
    • (2004) Journal of Computational Chemistry , vol.25 , pp. 1400-1415
    • Mackerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 66
    • 0002322469 scopus 로고
    • On a test of whether one of two random variables is stochastically larger than the other
    • Mann HB, Whitney DR. 1947. On a test of whether one of two random variables is stochastically larger than the other. The Annals of Mathematical Statistics 18:50-60. doi: 10.1214/aoms/1177730491
    • (1947) The Annals of Mathematical Statistics , vol.18 , pp. 50-60
    • Mann, H.B.1    Whitney, D.R.2
  • 67
    • 34548090201 scopus 로고    scopus 로고
    • The CLC ‘chloride channel’ family: Revelations from prokaryotes
    • Matulef K, Maduke M. 2007. The CLC ‘chloride channel’ family: revelations from prokaryotes. Molecular Membrane Biology 24:342-350. doi: 10.1080/09687680701413874
    • (2007) Molecular Membrane Biology , vol.24 , pp. 342-350
    • Matulef, K.1    Maduke, M.2
  • 68
    • 84941600274 scopus 로고    scopus 로고
    • In the beginning: A personal reminiscence on the origin and legacy of ClC-0, the ' torpedo cl - Channel’
    • Miller C. 2015. In the beginning: a personal reminiscence on the origin and legacy of ClC-0, the ' torpedo cl - channel’. The Journal of Physiology 593:4085-4090. doi: 10.1113/jphysiol.2014.286260
    • (2015) The Journal of Physiology , vol.593 , pp. 4085-4090
    • Miller, C.1
  • 69
    • 77949623101 scopus 로고    scopus 로고
    • Antiport mechanism for cl(-)/H(+) in ClC-ec1 from normal-mode analysis
    • Miloshevsky GV, Hassanein A, Jordan PC. 2010. Antiport mechanism for cl(-)/H(+) in ClC-ec1 from normal-mode analysis. Biophysical Journal 98:999-1008. doi: 10.1016/j.bpj.2009.11.035
    • (2010) Biophysical Journal , vol.98 , pp. 999-1008
    • Miloshevsky, G.V.1    Hassanein, A.2    Jordan, P.C.3
  • 70
    • 84900860340 scopus 로고    scopus 로고
    • Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter
    • Mishra S, Verhalen B, Stein RA, Wen PC, Tajkhorshid E, Mchaourab HS. 2014. Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter. eLife 3:e02740. doi: 10.7554/eLife.02740
    • (2014) eLife , vol.3
    • Mishra, S.1    Verhalen, B.2    Stein, R.A.3    Wen, P.C.4    Tajkhorshid, E.5    McHaourab, H.S.6
  • 72
    • 33748310543 scopus 로고    scopus 로고
    • Uncoupling of a CLC cl-/H+ exchange transporter by polyatomic anions
    • Nguitragool W, Miller C. 2006. Uncoupling of a CLC cl-/H+ exchange transporter by polyatomic anions. Journal of Molecular Biology 362:682-690. doi: 10.1016/j.jmb.2006.07.006
    • (2006) Journal of Molecular Biology , vol.362 , pp. 682-690
    • Nguitragool, W.1    Miller, C.2
  • 75
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • Nosé S. 1984. A unified formulation of the constant temperature molecular dynamics methods. The Journal of Chemical Physics 81:511-519. doi: 10.1063/1.447334
    • (1984) The Journal of Chemical Physics , vol.81 , pp. 511-519
    • Nosé, S.1
  • 76
    • 58149302956 scopus 로고    scopus 로고
    • Insights into the ClC-4 transport mechanism from studies of Zn2+ inhibition
    • Osteen JD, Mindell JA. 2008. Insights into the ClC-4 transport mechanism from studies of Zn2+ inhibition. Biophysical Journal 95:4668-4675. doi: 10.1529/biophysj.108.137158
    • (2008) Biophysical Journal , vol.95 , pp. 4668-4675
    • Osteen, J.D.1    Mindell, J.A.2
  • 77
    • 51249194404 scopus 로고
    • Contributions to the theory of active transport: II. the gate type non-carrier mechanism and generalizations concerning tracer flow, efficiency, and measurement of energy expenditure
    • Patlak CS. 1957. Contributions to the theory of active transport: II. the gate type non-carrier mechanism and generalizations concerning tracer flow, efficiency, and measurement of energy expenditure. The Bulletin of Mathematical Biophysics 19:209-235. doi: 10.1007/BF02477764
    • (1957) The Bulletin of Mathematical Biophysics , vol.19 , pp. 209-235
    • Patlak, C.S.1
  • 78
    • 84936768118 scopus 로고    scopus 로고
    • Structure and transport mechanism of the sodium/proton antiporter MjNhaP1
    • Paulino C, Wöhlert D, Kapotova E, Yildiz Ö, Kühlbrandt W. 2014. Structure and transport mechanism of the sodium/proton antiporter MjNhaP1. eLife 3:e03583. doi: 10.7554/eLife.03583
    • (2014) eLife , vol.3
    • Paulino, C.1    Wöhlert, D.2    Kapotova, E.3    Yildiz, E.4    Kühlbrandt, W.5
  • 79
    • 84868090870 scopus 로고    scopus 로고
    • Ubiquitin dynamics in complexes reveal molecular recognition mechanisms beyond induced fit and conformational selection
    • Peters JH, de Groot BL. 2012. Ubiquitin dynamics in complexes reveal molecular recognition mechanisms beyond induced fit and conformational selection. PLoS Computational Biology 8:e1002704. doi: 10.1371/journal.pcbi.1002704
    • (2012) PLoS Computational Biology , vol.8
    • Peters, J.H.1    de Groot, B.L.2
  • 81
    • 71449123048 scopus 로고    scopus 로고
    • Basis of substrate binding and conservation of selectivity in the CLC family of channels and transporters
    • Picollo A, Malvezzi M, Houtman JC, Accardi A. 2009. Basis of substrate binding and conservation of selectivity in the CLC family of channels and transporters. Nature Structural & Molecular Biology 16:1294-1301. doi: 10.1038/nsmb.1704
    • (2009) Nature Structural & Molecular Biology , vol.16 , pp. 1294-1301
    • Picollo, A.1    Malvezzi, M.2    Houtman, J.C.3    Accardi, A.4
  • 82
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo A, Pusch M. 2005. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436:420-423. doi: 10.1038/nature03720
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 83
    • 84860739823 scopus 로고    scopus 로고
    • Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic h+/Cl- exchanger
    • Picollo A, Xu Y, Johner N, Bernèche S, Accardi A. 2012. Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic h+/Cl- exchanger. Nature Structural & Molecular Biology 19:525-531. doi: 10.1038/nsmb.2277
    • (2012) Nature Structural & Molecular Biology , vol.19 , pp. 525-531
    • Picollo, A.1    Xu, Y.2    Johner, N.3    Bernèche, S.4    Accardi, A.5
  • 84
    • 84930526405 scopus 로고    scopus 로고
    • ClC-5: Physiological role and biophysical mechanisms
    • Pusch M, Zifarelli G. 2015. ClC-5: physiological role and biophysical mechanisms. Cell Calcium 58:57-66. doi: 10.1016/j.ceca.2014.09.007
    • (2015) Cell Calcium , vol.58 , pp. 57-66
    • Pusch, M.1    Zifarelli, G.2
  • 85
  • 86
    • 78650171241 scopus 로고    scopus 로고
    • Design, function and structure of a monomeric ClC transporter
    • Robertson JL, Kolmakova-Partensky L, Miller C. 2010. Design, function and structure of a monomeric ClC transporter. Nature 468:844-847. doi: 10.1038/nature09556
    • (2010) Nature , vol.468 , pp. 844-847
    • Robertson, J.L.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 87
    • 84886686229 scopus 로고    scopus 로고
    • How do transporters couple solute movements?
    • Rudnick G. 2013. How do transporters couple solute movements? Molecular Membrane Biology 30:355-359. doi: 10.3109/09687688.2013.842658
    • (2013) Molecular Membrane Biology , vol.30 , pp. 355-359
    • Rudnick, G.1
  • 88
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel O, Zdebik AA, Lourdel S, Jentsch TJ. 2005. Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436:424-427. doi: 10.1038/nature03860
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 89
    • 84944648082 scopus 로고
    • Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides
    • Shannon RD. 1976. Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides. Acta Crystallographica Section A 32:751-767. doi: 10.1107/S0567739476001551
    • (1976) Acta Crystallographica Section A , vol.32 , pp. 751-767
    • Shannon, R.D.1
  • 90
    • 84874249804 scopus 로고    scopus 로고
    • Common folds and transport mechanisms of secondary active transporters
    • Shi Y. 2013. Common folds and transport mechanisms of secondary active transporters. Annual Review of Biophysics 42:51-72. doi: 10.1146/annurev-biophys-083012-130429
    • (2013) Annual Review of Biophysics , vol.42 , pp. 51-72
    • Shi, Y.1
  • 91
    • 84930798684 scopus 로고    scopus 로고
    • Active transporters as enzymes: An energetic framework applied to major facilitator superfamily and ABC importer systems
    • Shilton BH. 2015. Active transporters as enzymes: an energetic framework applied to major facilitator superfamily and ABC importer systems. The Biochemical Journal 467:193-199. doi: 10.1042/BJ20140675
    • (2015) The Biochemical Journal , vol.467 , pp. 193-199
    • Shilton, B.H.1
  • 92
    • 37649021608 scopus 로고    scopus 로고
    • Global twisting motion of single molecular KcsA potassium channel upon gating
    • Shimizu H, Iwamoto M, Konno T, Nihei A, Sasaki YC, Oiki S. 2008. Global twisting motion of single molecular KcsA potassium channel upon gating. Cell 132:67-78. doi: 10.1016/j.cell.2007.11.040
    • (2008) Cell , vol.132 , pp. 67-78
    • Shimizu, H.1    Iwamoto, M.2    Konno, T.3    Nihei, A.4    Sasaki, Y.C.5    Oiki, S.6
  • 93
    • 33744926664 scopus 로고    scopus 로고
    • Common mechanism of pore opening shared by five different potassium channels
    • Shrivastava IH, Bahar I. 2006. Common mechanism of pore opening shared by five different potassium channels. Biophysical Journal 90:3929-3940. doi: 10.1529/biophysj.105.080093
    • (2006) Biophysical Journal , vol.90 , pp. 3929-3940
    • Shrivastava, I.H.1    Bahar, I.2
  • 94
    • 78649784550 scopus 로고    scopus 로고
    • Principal component and normal mode analysis of proteins; a quantitative comparison using the GroEL subunit
    • Skjaerven L, Martinez A, Reuter N. 2011. Principal component and normal mode analysis of proteins; a quantitative comparison using the GroEL subunit. Proteins 79:232-243. doi: 10.1002/prot.22875
    • (2011) Proteins , vol.79 , pp. 232-243
    • Skjaerven, L.1    Martinez, A.2    Reuter, N.3
  • 95
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • Smart OS, Neduvelil JG, Wang X, Wallace BA, Sansom MSP. 1996. HOLE: a program for the analysis of the pore dimensions of ion channel structural models. Journal of Molecular Graphics 14:354-360. doi: 10.1016/S0263-7855(97)00009-X
    • (1996) Journal of Molecular Graphics , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.P.5
  • 96
    • 84868129315 scopus 로고    scopus 로고
    • Cell biology and physiology of CLC chloride channels and transporters
    • Stauber T, Weinert S, Jentsch TJ. 2012. Cell biology and physiology of CLC chloride channels and transporters. Comprehensive Physiology 2:1701-1744. doi: 10.1002/cphy.c110038
    • (2012) Comprehensive Physiology , vol.2 , pp. 1701-1744
    • Stauber, T.1    Weinert, S.2    Jentsch, T.J.3
  • 97
    • 84945483989 scopus 로고    scopus 로고
    • A straightforward approach to the analysis of double electron-electron resonance data
    • Stein RA, Beth AH, Hustedt EJ. 2015. A straightforward approach to the analysis of double electron-electron resonance data. Methods in Enzymology 563:531-567. doi: 10.1016/bs.mie.2015.07.031
    • (2015) Methods in Enzymology , vol.563 , pp. 531-567
    • Stein, R.A.1    Beth, A.H.2    Hustedt, E.J.3
  • 99
    • 84908417266 scopus 로고    scopus 로고
    • CLC channel function and dysfunction in health and disease
    • Stölting G, Fischer M, Fahlke C. 2014. CLC channel function and dysfunction in health and disease. Frontiers in Physiology 5:378. doi: 10.3389/fphys.2014.00378
    • (2014) Frontiers in Physiology , vol.5 , pp. 378
    • Stölting, G.1    Fischer, M.2    Fahlke, C.3
  • 100
    • 0034906622 scopus 로고    scopus 로고
    • Analysis of a 10-ns molecular dynamics simulation of mouse acetylcholinesterase
    • Tai K, Shen T, Börjesson U, Philippopoulos M, McCammon JA. 2001. Analysis of a 10-ns molecular dynamics simulation of mouse acetylcholinesterase. Biophysical Journal 81:715-724. doi: 10.1016/S0006-3495(01)75736-0
    • (2001) Biophysical Journal , vol.81 , pp. 715-724
    • Tai, K.1    Shen, T.2    Börjesson, U.3    Philippopoulos, M.4    McCammon, J.A.5
  • 101
    • 33645884135 scopus 로고    scopus 로고
    • Spin relaxation measurements of electrostatic bias in intermolecular exploration
    • Teng CL, Bryant RG. 2006. Spin relaxation measurements of electrostatic bias in intermolecular exploration. Journal of Magnetic Resonance 179:199-205. doi: 10.1016/j.jmr.2005.12.001
    • (2006) Journal of Magnetic Resonance , vol.179 , pp. 199-205
    • Teng, C.L.1    Bryant, R.G.2
  • 103
    • 40249088362 scopus 로고    scopus 로고
    • Measuring the dynamic surface accessibility of RNA with the small paramagnetic molecule TEMPOL
    • Venditti V, Niccolai N, Butcher SE. 2008. Measuring the dynamic surface accessibility of RNA with the small paramagnetic molecule TEMPOL. Nucleic Acids Research 36:e20. doi: 10.1093/nar/gkm1062
    • (2008) Nucleic Acids Research , vol.36
    • Venditti, V.1    Niccolai, N.2    Butcher, S.E.3
  • 105
    • 68949143576 scopus 로고    scopus 로고
    • Proton transport pathway in the ClC cl-/H+ antiporter
    • Wang D, Voth GA. 2009. Proton transport pathway in the ClC cl-/H+ antiporter. Biophysical Journal 97:121-131. doi: 10.1016/j.bpj.2009.04.038
    • (2009) Biophysical Journal , vol.97 , pp. 121-131
    • Wang, D.1    Voth, G.A.2
  • 106
    • 84904599245 scopus 로고    scopus 로고
    • Ring flips revisited: 13 c relaxation dispersion measurements of aromatic side chain dynamics and activation barriers in basic pancreatic trypsin inhibitor
    • Weininger U, Modig K, Akke M. 2014. Ring flips revisited: 13 c relaxation dispersion measurements of aromatic side chain dynamics and activation barriers in basic pancreatic trypsin inhibitor. Biochemistry 53:4519-4525. doi: 10.1021/bi500462k
    • (2014) Biochemistry , vol.53 , pp. 4519-4525
    • Weininger, U.1    Modig, K.2    Akke, M.3
  • 107
    • 38949218425 scopus 로고    scopus 로고
    • Close correspondence between the motions from principal component analysis of multiple HIV-1 protease structures and elastic network modes
    • Yang L, Song G, Carriquiry A, Jernigan RL. 2008. Close correspondence between the motions from principal component analysis of multiple HIV-1 protease structures and elastic network modes. Structure 16:321-330. doi: 10.1016/j.str.2007.12.011
    • (2008) Structure , vol.16 , pp. 321-330
    • Yang, L.1    Song, G.2    Carriquiry, A.3    Jernigan, R.L.4
  • 108
    • 84885433421 scopus 로고    scopus 로고
    • Conformational analysis of NMDA receptor GluN1, GluN2, and GluN3 ligand-binding domains reveals subtype-specific characteristics
    • Yao Y, Belcher J, Berger AJ, Mayer ML, Lau AY. 2013. Conformational analysis of NMDA receptor GluN1, GluN2, and GluN3 ligand-binding domains reveals subtype-specific characteristics. Structure 21:1788-1799. doi: 10.1016/j.str.2013.07.011
    • (2013) Structure , vol.21 , pp. 1788-1799
    • Yao, Y.1    Belcher, J.2    Berger, A.J.3    Mayer, M.L.4    Lau, A.Y.5
  • 109
    • 0029937870 scopus 로고    scopus 로고
    • Hydrophilicity of cavities in proteins
    • Zhang L, Hermans J. 1996. Hydrophilicity of cavities in proteins. Proteins: Structure, Function, and Genetics 24: 433-438. doi: 10.1002/(SICI)1097-0134(199604)24:4<433::AID-PROT3>3.0.CO;2-F
    • (1996) Proteins: Structure, Function, and Genetics , vol.24 , pp. 433-438
    • Zhang, L.1    Hermans, J.2
  • 110
    • 65649120105 scopus 로고    scopus 로고
    • CLC-7: A potential therapeutic target for the treatment of osteoporosis and neurodegeneration
    • Zhao Q, Wei Q, He A, Jia R, Xiao Y. 2009. CLC-7: a potential therapeutic target for the treatment of osteoporosis and neurodegeneration. Biochemical and Biophysical Research Communications 384:277-279. doi: 10.1016/j.bbrc.2009.04.088
    • (2009) Biochemical and Biophysical Research Communications , vol.384 , pp. 277-279
    • Zhao, Q.1    Wei, Q.2    He, A.3    Jia, R.4    Xiao, Y.5
  • 111
    • 0344826573 scopus 로고    scopus 로고
    • A CLC-type chloride channel gene is required for laccase activity and virulence in cryptococcus neoformans
    • Zhu X, Williamson PR. 2003. A CLC-type chloride channel gene is required for laccase activity and virulence in cryptococcus neoformans. Molecular Microbiology 50:1271-1281. doi: 10.1046/j.1365-2958.2003.03752.x
    • (2003) Molecular Microbiology , vol.50 , pp. 1271-1281
    • Zhu, X.1    Williamson, P.R.2
  • 112
    • 34548852606 scopus 로고    scopus 로고
    • CLC chloride channels and transporters: A biophysical and physiological perspective
    • Zifarelli G, Pusch M. 2007. CLC chloride channels and transporters: a biophysical and physiological perspective. Reviews of Physiology, Biochemistry and Pharmacology 158:23-76. doi: 10.1007/112_2006_0605
    • (2007) Reviews of Physiology, Biochemistry and Pharmacology , vol.158 , pp. 23-76
    • Zifarelli, G.1    Pusch, M.2
  • 113
    • 84941599754 scopus 로고    scopus 로고
    • A tale of two CLCs: Biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes
    • Zifarelli G. 2015. A tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes. The Journal of Physiology 593:4139-4150. doi: 10.1113/JP270604
    • (2015) The Journal of Physiology , vol.593 , pp. 4139-4150
    • Zifarelli, G.1


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