메뉴 건너뛰기




Volumn 19, Issue 5, 2012, Pages 525-531

Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H +/Cl - exchanger

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE; CHLORINE; HYDROGEN;

EID: 84860739823     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2277     Document Type: Article
Times cited : (66)

References (60)
  • 1
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. Simple allosteric model for membrane pumps. Nature 211, 969-970 (1966).
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 2
    • 0024534816 scopus 로고
    • Structure and function of the red blood cell anion transport protein
    • Jennings, M.L. Structure and function of the red blood cell anion transport protein. Annu. Rev. Biophys. Biophys. Chem. 18, 397-430 (1989).
    • (1989) Annu. Rev. Biophys. Biophys. Chem. , vol.18 , pp. 397-430
    • Jennings, M.L.1
  • 3
    • 34547902820 scopus 로고    scopus 로고
    • Mechanism of Na +H+ antiporting
    • Arkin, I.T. et al. Mechanism of Na +H+ antiporting. Science 317, 799-803 (2007).
    • (2007) Science , vol.317 , pp. 799-803
    • Arkin, I.T.1
  • 4
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare, D., Oldham, M.L., Orelle, C., Davidson, A.L. & Chen, J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell 33, 528-536 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 5
    • 77951585158 scopus 로고    scopus 로고
    • Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1
    • Shimamura, T. et al. Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1. Science 328, 470-473 (2010).
    • (2010) Science , vol.328 , pp. 470-473
    • Shimamura, T.1
  • 7
    • 79952738070 scopus 로고    scopus 로고
    • The alternating-access mechanism of MFS transporters arises from inverted-topology repeats
    • Radestock, S. & Forrest, L.R. The alternating-access mechanism of MFS transporters arises from inverted-topology repeats. J. Mol. Biol. 407, 698-715 (2011).
    • (2011) J. Mol. Biol. , vol.407 , pp. 698-715
    • Radestock, S.1    Forrest, L.R.2
  • 8
    • 0026653443 scopus 로고
    • Ferret red cells: Na/Ca exchange and Na-K-Cl cotransport
    • Milanick, M.A. Ferret red cells: Na/Ca exchange and Na-K-Cl cotransport. Comp. Biochem. Physiol. Comp. Physiol. 102, 619-624 (1992).
    • (1992) Comp. Biochem. Physiol. Comp. Physiol. , vol.102 , pp. 619-624
    • Milanick, M.A.1
  • 9
    • 0028882542 scopus 로고
    • A conserved glutamate is responsible for ion selectivity and pH dependence of the mammalian anion exchangers AE1 and AE2
    • Sekler, I., Lo, R.S. & Kopito, R.R. A conserved glutamate is responsible for ion selectivity and pH dependence of the mammalian anion exchangers AE1 and AE2. J. Biol. Chem. 270, 28751-28758 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 28751-28758
    • Sekler, I.1    Lo, R.S.2    Kopito, R.R.3
  • 10
    • 60549109436 scopus 로고    scopus 로고
    • The squid axon Na +Ca2+ exchanger shows ping-pong kinetics only when the Cai-regulatory site is saturated
    • Beaugé, L. & DiPolo, R. The squid axon Na +Ca2+ exchanger shows ping-pong kinetics only when the Cai-regulatory site is saturated. Cell. Physiol. Biochem. 23, 37-42 (2009).
    • (2009) Cell. Physiol. Biochem. , vol.23 , pp. 37-42
    • Beaugé, L.1    Dipolo, R.2
  • 11
    • 36749095723 scopus 로고    scopus 로고
    • The fast release of sticky protons: Kinetics of substrate binding and proton release in a multidrug transporter
    • Adam, Y., Tayer, N., Rotem, D., Schreiber, G. & Schuldiner, S. The fast release of sticky protons: kinetics of substrate binding and proton release in a multidrug transporter. Proc. Natl. Acad. Sci. USA 104, 17989-17994 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17989-17994
    • Adam, Y.1    Tayer, N.2    Rotem, D.3    Schreiber, G.4    Schuldiner, S.5
  • 12
    • 0026496916 scopus 로고
    • A novel method to differentiate between ping-pong and simultaneous exchange kinetics and its application to the anion exchanger of the HL60 cell
    • Restrepo, D., Cronise, B.L., Snyder, R.B. & Knauf, P.A. A novel method to differentiate between ping-pong and simultaneous exchange kinetics and its application to the anion exchanger of the HL60 cell. J. Gen. Physiol. 100, 825-846 (1992).
    • (1992) J. Gen. Physiol. , vol.100 , pp. 825-846
    • Restrepo, D.1    Cronise, B.L.2    Snyder, R.B.3    Knauf, P.A.4
  • 14
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • Dutzler, R., Campbell, E.B., Cadene, M., Chait, B.T. & MacKinnon, R. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415, 287-294 (2002).
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 15
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J. et al. Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615 (2003).
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1
  • 16
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homolog from Pyrococcus horikoshii
    • Yernool, D., Boudker, O., Jin, Y. & Gouaux, E. Structure of a glutamate transporter homolog from Pyrococcus horikoshii. Nature 431, 811-818 (2004).
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 18
    • 37249088547 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump
    • Morth, J.P. et al. Crystal structure of the sodium-potassium pump. Nature 450, 1043-1049 (2007).
    • (2007) Nature , vol.450 , pp. 1043-1049
    • Morth, J.P.1
  • 19
    • 37249043376 scopus 로고    scopus 로고
    • The structural basis of calcium transport by the calcium pump
    • Olesen, C. et al. The structural basis of calcium transport by the calcium pump. Nature 450, 1036-1042 (2007).
    • (2007) Nature , vol.450 , pp. 1036-1042
    • Olesen, C.1
  • 20
    • 69249220125 scopus 로고    scopus 로고
    • Structure of a prokaryotic virtual proton pump at 3.2-Å resolution
    • Fang, Y. et al. Structure of a prokaryotic virtual proton pump at 3.2-Å resolution. Nature 460, 1040-1043 (2009).
    • (2009) Nature , vol.460 , pp. 1040-1043
    • Fang, Y.1
  • 23
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel, O., Zdebik, A.A., Lourdel, S. & Jentsch, T.J. Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436, 424-427 (2005).
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 24
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo, A. & Pusch, M. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436, 420-423 (2005).
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 25
    • 33747858034 scopus 로고    scopus 로고
    • The nitrate/proton antiporter AtCLCa mediates nitrate accumulation in plant vacuoles
    • De Angeli, A. et al. The nitrate/proton antiporter AtCLCa mediates nitrate accumulation in plant vacuoles. Nature 442, 939-942 (2006).
    • (2006) Nature , vol.442 , pp. 939-942
    • De Angeli, A.1
  • 26
    • 44849107047 scopus 로고    scopus 로고
    • + antiporter ClC-7 is the primary chloride permeation pathway in lysosomes
    • + antiporter ClC-7 is the primary chloride permeation pathway in lysosomes. Nature 453, 788 (2008).
    • (2008) Nature , vol.453 , pp. 788
    • Graves, A.R.1    Curran, P.2    Smith, C.3    Mindell, J.4
  • 27
    • 38349134206 scopus 로고    scopus 로고
    • Overexpression of CLC-3 in HEK293T cells yields novel currents that are pH dependent
    • Matsuda, J.J. et al. Overexpression of CLC-3 in HEK293T cells yields novel currents that are pH dependent. Am. J. Physiol. Cell Physiol. 294, C251-262 (2008).
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294
    • Matsuda, J.J.1
  • 29
    • 78049362741 scopus 로고    scopus 로고
    • Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle
    • Feng, L., Campbell, E.B., Hsiung, Y. & MacKinnon, R. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330, 635-641 (2010).
    • (2010) Science , vol.330 , pp. 635-641
    • Feng, L.1    Campbell, E.B.2    Hsiung, Y.3    MacKinnon, R.4
  • 30
    • 39849105844 scopus 로고    scopus 로고
    • Determinants of anion-proton coupling in mammalian endosomal CLC proteins
    • Zdebik, A.A. et al. Determinants of anion-proton coupling in mammalian endosomal CLC proteins. J. Biol. Chem. 283, 4219-4227 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 4219-4227
    • Zdebik, A.A.1
  • 31
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., Campbell, E.B. & MacKinnon, R. Gating the selectivity filter in ClC chloride channels. Science 300, 108-112 (2003).
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 32
    • 77953808359 scopus 로고    scopus 로고
    • CLC channels and transporters: Proteins with borderline personalities
    • Accardi, A. & Picollo, A. CLC channels and transporters: proteins with borderline personalities. Biochim. Biophys. Acta 1798, 1457-1464 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1457-1464
    • Accardi, A.1    Picollo, A.2
  • 33
    • 77953555147 scopus 로고    scopus 로고
    • Endosomal chloride-proton exchange rather than chloride conductance is crucial for renal endocytosis
    • Novarino, G., Weinert, S., Rickheit, G. & Jentsch, T.J. Endosomal chloride-proton exchange rather than chloride conductance is crucial for renal endocytosis. Science 328, 1398-1401 (2010).
    • (2010) Science , vol.328 , pp. 1398-1401
    • Novarino, G.1    Weinert, S.2    Rickheit, G.3    Jentsch, T.J.4
  • 34
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
    • Baker, B.M. & Murphy, K.P. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys. J. 71, 2049-2055 (1996).
    • (1996) Biophys. J. , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 35
    • 0033997038 scopus 로고    scopus 로고
    • Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA
    • Petrosian, S.A. & Makhatadze, G.I. Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. Protein Sci. 9, 387-394 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 387-394
    • Petrosian, S.A.1    Makhatadze, G.I.2
  • 36
    • 0033815251 scopus 로고    scopus 로고
    • Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor
    • Velazquez-Campoy, A. et al. Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor. Protein Sci. 9, 1801-1809 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 1801-1809
    • Velazquez-Campoy, A.1
  • 37
    • 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, J. & Accardi, A. Basis of substrate binding and conservation of selectivity in the CLC family of channels and transporters. Nat. Struct. Mol. Biol. 16, 1294-1301 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1294-1301
    • Picollo, A.1    Malvezzi, M.2    Houtman, J.3    Accardi, A.4
  • 38
    • 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. Synergism between halide binding and proton transport in a CLC-type exchanger. J. Mol. Biol. 362, 691-699 (2006).
    • (2006) J. Mol. Biol. , vol.362 , pp. 691-699
    • Accardi, A.1    Lobet, S.2    Williams, C.3    Miller, C.4    Dutzler, R.5
  • 39
    • 33947720910 scopus 로고    scopus 로고
    • + exchange transporter
    • + exchange transporter. J. Gen. Physiol. 129, 317-329 (2007).
    • (2007) J. Gen. Physiol. , vol.129 , pp. 317-329
    • Walden, M.1
  • 40
    • 0037126294 scopus 로고    scopus 로고
    • A biological role for prokaryotic ClC chloride channels
    • Iyer, R., Iverson, T.M., Accardi, A. & Miller, C. A biological role for prokaryotic ClC chloride channels. Nature 419, 715-718 (2002).
    • (2002) Nature , vol.419 , pp. 715-718
    • Iyer, R.1    Iverson, T.M.2    Accardi, A.3    Miller, C.4
  • 42
    • 33748310543 scopus 로고    scopus 로고
    • + exchange transporter by polyatomic anions
    • + exchange transporter by polyatomic anions. J. Mol. Biol. 362, 682-690 (2006).
    • (2006) J. Mol. Biol. , vol.362 , pp. 682-690
    • Nguitragool, W.1    Miller, C.2
  • 43
    • 30444442312 scopus 로고    scopus 로고
    • Ion-binding properties of the ClC chloride selectivity filter
    • Lobet, S. & Dutzler, R. Ion-binding properties of the ClC chloride selectivity filter. EMBO J. 25, 24-33 (2006).
    • (2006) EMBO J. , vol.25 , pp. 24-33
    • Lobet, S.1    Dutzler, R.2
  • 45
    • 59649097040 scopus 로고    scopus 로고
    • + antiporter by a single point mutation
    • + antiporter by a single point mutation. EMBO J. 28, 175-182 (2009).
    • (2009) EMBO J. , vol.28 , pp. 175-182
    • Zifarelli, G.1    Pusch, M.2
  • 46
    • 0025270712 scopus 로고
    • Steady-state coupling of ion-channel conformations to a transmembrane ion gradient
    • Richard, E.A. & Miller, C. Steady-state coupling of ion-channel conformations to a transmembrane ion gradient. Science 247, 1208-1210 (1990).
    • (1990) Science , vol.247 , pp. 1208-1210
    • Richard, E.A.1    Miller, C.2
  • 48
    • 0042377364 scopus 로고    scopus 로고
    • Side-chain charge effects and conductance determinants in the pore of ClC-0 chloride channels
    • Chen, M.F. & Chen, T.Y. Side-chain charge effects and conductance determinants in the pore of ClC-0 chloride channels. J. Gen. Physiol. 122, 133-145 (2003).
    • (2003) J. Gen. Physiol. , vol.122 , pp. 133-145
    • Chen, M.F.1    Chen, T.Y.2
  • 51
    • 0031670461 scopus 로고    scopus 로고
    • Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride
    • Fukada, H. & Takahashi, K. Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride. Proteins 33, 159-166 (1998).
    • (1998) Proteins , vol.33 , pp. 159-166
    • Fukada, H.1    Takahashi, K.2
  • 52
    • 0032692857 scopus 로고    scopus 로고
    • High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel
    • Maduke, M., Pheasant, D.J. & Miller, C. High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel. J. Gen. Physiol. 114, 713-722 (1999).
    • (1999) J. Gen. Physiol. , vol.114 , pp. 713-722
    • Maduke, M.1    Pheasant, D.J.2    Miller, C.3
  • 53
    • 47149096704 scopus 로고    scopus 로고
    • CHARMM-GUI: A web-based graphical user interface for CHARMM
    • Jo, S., Kim, T., Iyer, V.G. & Im, W. CHARMM-GUI: a web-based graphical user interface for CHARMM. J. Comput. Chem. 29, 1859-1865 (2008).
    • (2008) J. Comput. Chem. , vol.29 , pp. 1859-1865
    • Jo, S.1    Kim, T.2    Iyer, V.G.3    Im, W.4
  • 54
    • 67650500988 scopus 로고    scopus 로고
    • CHARMM: The biomolecular simulation program
    • Brooks, B.R. et al. CHARMM: the biomolecular simulation program. J. Comput. Chem. 30, 1545-1614 (2009).
    • (2009) J. Comput. Chem. , vol.30 , pp. 1545-1614
    • Brooks, B.R.1
  • 55
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A.D. Jr. et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 102, 3586-3616 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell Jr., A.D.1
  • 56
    • 78651250118 scopus 로고    scopus 로고
    • Absence of ion-binding affinity in the putatively inactivated low-[K+] structure of the KcsA potassium channel
    • Boiteux, C. & Bernèche, S. Absence of ion-binding affinity in the putatively inactivated low-[K+] structure of the KcsA potassium channel. Structure 19, 70-79 (2011).
    • (2011) Structure , vol.19 , pp. 70-79
    • Boiteux, C.1    Bernèche, S.2
  • 57
    • 0035277126 scopus 로고    scopus 로고
    • Extension to the weighted histogram analysis method: Combining umbrella sampling with free energy calculations
    • Souaille, M. & Roux, B. Extension to the weighted histogram analysis method: combining umbrella sampling with free energy calculations. Comput. Phys. Commun. 135, 40-57 (2001).
    • (2001) Comput. Phys. Commun. , vol.135 , pp. 40-57
    • Souaille, M.1    Roux, B.2
  • 58
    • 52949088587 scopus 로고    scopus 로고
    • Statistically optimal analysis of samples from multiple equilibrium states
    • Shirts, M.R. & Chodera, J.D. Statistically optimal analysis of samples from multiple equilibrium states. J. Chem. Phys. 129, 124105 (2008).
    • (2008) J. Chem. Phys. , vol.129 , pp. 124105
    • Shirts, M.R.1    Chodera, J.D.2
  • 59
    • 77955577540 scopus 로고    scopus 로고
    • Good practices in free-energy calculations
    • Pohorille, A., Jarzynski, C. & Chipot, C. Good practices in free-energy calculations. J. Phys. Chem. B 114, 10235-10253 (2010).
    • (2010) J. Phys. Chem. B , vol.114 , pp. 10235-10253
    • Pohorille, A.1    Jarzynski, C.2    Chipot, C.3
  • 60
    • 2542437774 scopus 로고    scopus 로고
    • Electrostatics of ion stabilization in a ClC chloride channel homolog from Escherichia coli
    • Faraldo-Gómez, J.D. & Roux, B. Electrostatics of ion stabilization in a ClC chloride channel homolog from Escherichia coli. J. Mol. Biol. 339, 981-1000 (2004).
    • (2004) J. Mol. Biol. , vol.339 , pp. 981-1000
    • Faraldo-Gómez, J.D.1    Roux, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.