메뉴 건너뛰기




Volumn 20, Issue 5, 2013, Pages 634-640

Binding thermodynamics of a glutamate transporter homolog

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; GLUTAMATE TRANSPORTER; SODIUM ION;

EID: 85027948926     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2548     Document Type: Article
Times cited : (74)

References (47)
  • 1
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • Forrest, L.R., Kramer, R. & Ziegler, C. The structural basis of secondary active transport mechanisms. Biochim. Biophys. Acta 1807, 167-188 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Kramer, R.2    Ziegler, C.3
  • 2
    • 4344647988 scopus 로고    scopus 로고
    • Binding affinity of lactose permease is not altered by the H+ electrochemical gradient
    • Guan, L. & Kaback, H.R. Binding affinity of lactose permease is not altered by the H+ electrochemical gradient. Proc. Natl. Acad. Sci. USA 101, 12148-12152 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12148-12152
    • Guan, L.1    Kaback, H.R.2
  • 3
    • 67650526059 scopus 로고    scopus 로고
    • Functional characterization of a Na+-dependent aspartate transporter from Pyrococcus horikoshii
    • Ryan, R.M., Compton, E.L. & Mindell, J.A. Functional characterization of a Na+-dependent aspartate transporter from Pyrococcus horikoshii. J. Biol. Chem. 284, 17540-17548 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 17540-17548
    • Ryan, R.M.1    Compton, E.L.2    Mindell, J.A.3
  • 4
    • 77951680965 scopus 로고    scopus 로고
    • Na+:aspartate coupling stoichiometry in the glutamate transporter homologue GltPh
    • Groeneveld, M. & Slotboom, D.J. Na+:aspartate coupling stoichiometry in the glutamate transporter homologue GltPh. Biochemistry 49, 3511-3513 (2010).
    • (2010) Biochemistry , vol.49 , pp. 3511-3513
    • Groeneveld, M.1    Slotboom, D.J.2
  • 5
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool, D., Boudker, O., Jin, Y. & Gouaux, E. Structure of a glutamate transporter homologue 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
  • 6
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker, O., Ryan, R.M., Yernool, D., Shimamoto, K. & Gouaux, E. Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445, 387-393 (2007).
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 7
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • Reyes, N., Ginter, C. & Boudker, O. Transport mechanism of a bacterial homologue of glutamate transporters. Nature 462, 880-885 (2009).
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 8
    • 84857992685 scopus 로고    scopus 로고
    • Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog
    • Verdon, G. & Boudker, O. Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog. Nat. Struct. Mol. Biol. 19, 355-357 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 355-357
    • Verdon, G.1    Boudker, O.2
  • 9
    • 84861204243 scopus 로고    scopus 로고
    • Conserved asparagine residue located in binding pocket controls cation selectivity and substrate interactions in neuronal glutamate transporter
    • Teichman, S., Qu, S. & Kanner, B.I. Conserved asparagine residue located in binding pocket controls cation selectivity and substrate interactions in neuronal glutamate transporter. J Biol. Chem. 287, 17198-17205 (2012).
    • (2012) J Biol. Chem. , vol.287 , pp. 17198-17205
    • Teichman, S.1    Qu, S.2    Kanner, B.I.3
  • 10
    • 77956527543 scopus 로고    scopus 로고
    • Identification of the third Na+ site and the sequence of extracellular binding events in the glutamate transporter
    • Huang, Z. & Tajkhorshid, E. Identification of the third Na+ site and the sequence of extracellular binding events in the glutamate transporter. Biophys. J. 99, 1416-1425 (2010).
    • (2010) Biophys. J. , vol.99 , pp. 1416-1425
    • Huang, Z.1    Tajkhorshid, E.2
  • 11
    • 77956362466 scopus 로고    scopus 로고
    • Evidence for a third sodium-binding site in glutamate transporters suggests an ion/substrate coupling model
    • Larsson, H.P. et al. Evidence for a third sodium-binding site in glutamate transporters suggests an ion/substrate coupling model. Proc. Natl. Acad. Sci. USA 107, 13912-13917 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 13912-13917
    • Larsson, H.P.1
  • 12
    • 77952907248 scopus 로고    scopus 로고
    • Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101
    • Tao, Z. et al. Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101. J. Biol. Chem. 285, 17725-17733 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 17725-17733
    • Tao, Z.1
  • 13
    • 33748765517 scopus 로고    scopus 로고
    • Multiple consequences of mutating two conserved ?-bridge forming residues in the translocation cycle of a neuronal glutamate transporter
    • Rosental, N., Bendahan, A. & Kanner, B.I. Multiple consequences of mutating two conserved ?-bridge forming residues in the translocation cycle of a neuronal glutamate transporter. J. Biol. Chem. 281, 27905-27915 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 27905-27915
    • Rosental, N.1    Bendahan, A.2    Kanner, B.I.3
  • 14
    • 61449430457 scopus 로고    scopus 로고
    • Interactions of alkali cations with glutamate transporters
    • Holley, D.C. & Kavanaugh, M.P. Interactions of alkali cations with glutamate transporters. Phil. Trans. R. Soc. Lond. B 364, 155-161 (2009).
    • (2009) Phil. Trans. R. Soc. Lond. B , vol.364 , pp. 155-161
    • Holley, D.C.1    Kavanaugh, M.P.2
  • 15
    • 84858110981 scopus 로고    scopus 로고
    • Position of the third Na+ site in the aspartate transporter GltPh and the human glutamate transporter, EAAT1
    • Bastug, T. et al. Position of the third Na+ site in the aspartate transporter GltPh and the human glutamate transporter, EAAT1. PLoS ONE 7, e33058 (2012).
    • (2012) PLoS ONE , vol.7
    • Bastug, T.1
  • 16
    • 51649088013 scopus 로고    scopus 로고
    • Dynamics of the extracellular gate and ion-substrate coupling in the glutamate transporter
    • Huang, Z. & Tajkhorshid, E. Dynamics of the extracellular gate and ion-substrate coupling in the glutamate transporter. Biophys. J. 95, 2292-2300 (2008).
    • (2008) Biophys. J. , vol.95 , pp. 2292-2300
    • Huang, Z.1    Tajkhorshid, E.2
  • 17
    • 57649119782 scopus 로고    scopus 로고
    • Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter
    • Shrivastava, I.H., Jiang, J., Amara, S.G. & Bahar, I. Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter. J. Biol. Chem. 283, 28680-28690 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 28680-28690
    • Shrivastava, I.H.1    Jiang, J.2    Amara, S.G.3    Bahar, I.4
  • 18
    • 79955780433 scopus 로고    scopus 로고
    • Opposite movement of the external gate of a glutamate transporter homolog upon binding cotransported sodium compared with substrate
    • Focke, P.J., Moenne-Loccoz, P. & Larsson, H.P. Opposite movement of the external gate of a glutamate transporter homolog upon binding cotransported sodium compared with substrate. J. Neurosci. 31, 6255-6262 (2011).
    • (2011) J. Neurosci. , vol.31 , pp. 6255-6262
    • Focke, P.J.1    Moenne-Loccoz, P.2    Larsson, H.P.3
  • 19
    • 70349785247 scopus 로고    scopus 로고
    • Investigation of electrogenic partial reactions in detergent-solubilized Na,K-ATPase
    • Habeck, M., Cirri, E., Katz, A., Karlish, S.J. & Apell, H.J. Investigation of electrogenic partial reactions in detergent-solubilized Na,K-ATPase. Biochemistry 48, 9147-9155 (2009).
    • (2009) Biochemistry , vol.48 , pp. 9147-9155
    • Habeck, M.1    Cirri, E.2    Katz, A.3    Karlish, S.J.4    Apell, H.J.5
  • 20
    • 0036468487 scopus 로고    scopus 로고
    • Detection of charge movements in ion pumps by a family of styryl dyes
    • Pedersen, M. et al. Detection of charge movements in ion pumps by a family of styryl dyes. J. Membr. Biol. 185, 221-236 (2002).
    • (2002) J. Membr. Biol. , vol.185 , pp. 221-236
    • Pedersen, M.1
  • 21
    • 0028904415 scopus 로고
    • Voltage sensitivity of the fluorescent probe RH421 in a model membrane system
    • Clarke, R.J., Zouni, A. & Holzwarth, J.F. Voltage sensitivity of the fluorescent probe RH421 in a model membrane system. Biophys. J. 68, 1406-1415 (1995).
    • (1995) Biophys. J. , vol.68 , pp. 1406-1415
    • Clarke, R.J.1    Zouni, A.2    Holzwarth, J.F.3
  • 22
    • 55349092991 scopus 로고    scopus 로고
    • Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter
    • Weyand, S. et al. Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter. Science 322, 709-713 (2008).
    • (2008) Science , vol.322 , pp. 709-713
    • Weyand, S.1
  • 23
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue, N. & Kavanaugh, M.P. Flux coupling in a neuronal glutamate transporter. Nature 383, 634-637 (1996).
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 24
    • 0032400828 scopus 로고    scopus 로고
    • Stoichiometry of the glial glutamate transporter GLT-1 expressed inducibly in a Chinese hamster ovary cell line selected for low endogenous Na+-dependent glutamate uptake
    • Levy, L.M., Warr, O. & Attwell, D. Stoichiometry of the glial glutamate transporter GLT-1 expressed inducibly in a Chinese hamster ovary cell line selected for low endogenous Na+-dependent glutamate uptake. J. Neurosci. 18, 9620-9628 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 9620-9628
    • Levy, L.M.1    Warr, O.2    Attwell, D.3
  • 25
    • 33751326571 scopus 로고    scopus 로고
    • The ionic stoichiometry of the GLAST glutamate transporter in salamander retinal glia
    • Owe, S.G., Marcaggi, P. & Attwell, D. The ionic stoichiometry of the GLAST glutamate transporter in salamander retinal glia. J. Physiol. 577, 591-599 (2006).
    • (2006) J. Physiol. , vol.577 , pp. 591-599
    • Owe, S.G.1    Marcaggi, P.2    Attwell, D.3
  • 26
    • 36749058985 scopus 로고    scopus 로고
    • Transport direction determines the kinetics of substrate transport by the glutamate transporter EAAC1
    • Zhang, Z. et al. Transport direction determines the kinetics of substrate transport by the glutamate transporter EAAC1. Proc. Natl. Acad. Sci. USA 104, 18025-18030 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18025-18030
    • Zhang, Z.1
  • 27
    • 49149120836 scopus 로고    scopus 로고
    • Synthesis and preliminary pharmacological evaluation of novel derivatives of l-?-threo-benzylaspartate as inhibitors of the neuronal glutamate transporter EAAT3
    • Mavencamp, T.L., Rhoderick, J.F., Bridges, R.J. & Esslinger, C.S. Synthesis and preliminary pharmacological evaluation of novel derivatives of l-?-threo-benzylaspartate as inhibitors of the neuronal glutamate transporter EAAT3. Bioorg. Med. Chem. 16, 7740-7748 (2008).
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 7740-7748
    • Mavencamp, T.L.1    Rhoderick, J.F.2    Bridges, R.J.3    Esslinger, C.S.4
  • 28
    • 0031909675 scopus 로고    scopus 로고
    • Dl-threo-?-benzyloxyaspartate, a potent blocker of excitatory amino acid transporters
    • Shimamoto, K. et al. dl-threo-?-benzyloxyaspartate, a potent blocker of excitatory amino acid transporters. Mol. Pharmacol. 53, 195-201 (1998).
    • (1998) Mol. Pharmacol. , vol.53 , pp. 195-201
    • Shimamoto, K.1
  • 29
    • 0034613643 scopus 로고    scopus 로고
    • Syntheses of optically pure ?-hydroxyaspartate derivatives as glutamate transporter blockers
    • Shimamoto, K. et al. Syntheses of optically pure ?-hydroxyaspartate derivatives as glutamate transporter blockers. Bioorg. Med. Chem. Lett. 10, 2407-2410 (2000).
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 2407-2410
    • Shimamoto, K.1
  • 31
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson, A.D. & Murphy, K.P. Protein structure and the energetics of protein stability. Chem. Rev. 97, 1251-1268 (1997).
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1268
    • Robertson, A.D.1    Murphy, K.P.2
  • 32
    • 0034971963 scopus 로고    scopus 로고
    • Heat capacity changes upon burial of polar and nonpolar groups in proteins
    • Loladze, V.V., Ermolenko, D.N. & Makhatadze, G.I. Heat capacity changes upon burial of polar and nonpolar groups in proteins. Protein Sci. 10, 1343-1352 (2001).
    • (2001) Protein Sci. , vol.10 , pp. 1343-1352
    • Loladze, V.V.1    Ermolenko, D.N.2    Makhatadze, G.I.3
  • 34
    • 79951619800 scopus 로고    scopus 로고
    • The mechanism of substrate release by the aspartate transporter GltPh: Insights from simulations
    • DeChancie, J., Shrivastava, I.H. & Bahar, I. The mechanism of substrate release by the aspartate transporter GltPh: insights from simulations. Mol. Biosyst. 7, 832-842 (2011).
    • (2011) Mol. Biosyst. , vol.7 , pp. 832-842
    • Dechancie, J.1    Shrivastava, I.H.2    Bahar, I.3
  • 35
    • 1042298819 scopus 로고    scopus 로고
    • Heat capacity effects of water molecules and ions at a protein-DNA interface
    • Bergqvist, S., Williams, M.A., O'Brien, R. & Ladbury, J.E. Heat capacity effects of water molecules and ions at a protein-DNA interface. J. Mol. Biol. 336, 829-842 (2004).
    • (2004) J. Mol. Biol. , vol.336 , pp. 829-842
    • Bergqvist, S.1    Williams, M.A.2    O'Brien, R.3    Ladbury, J.E.4
  • 36
    • 0037062633 scopus 로고    scopus 로고
    • Van't Hoff and calorimetric enthalpies II: Effects of linked equilibria
    • Horn, J.R., Brandts, J.F. & Murphy, K.P. van't Hoff and calorimetric enthalpies II: effects of linked equilibria. Biochemistry 41, 7501-7507 (2002).
    • (2002) Biochemistry , vol.41 , pp. 7501-7507
    • Horn, J.R.1    Brandts, J.F.2    Murphy, K.P.3
  • 37
    • 80052323661 scopus 로고    scopus 로고
    • Rigidification of the autolysis loop enhances Na+ binding to thrombin
    • Pozzi, N., Chen, R., Chen, Z., Bah, A. & Di Cera, E. Rigidification of the autolysis loop enhances Na+ binding to thrombin. Biophys. Chem. 159, 6-13 (2011).
    • (2011) Biophys. Chem. , vol.159 , pp. 6-13
    • Pozzi, N.1    Chen, R.2    Chen, Z.3    Bah, A.4    Di Cera, E.5
  • 38
    • 0034255034 scopus 로고    scopus 로고
    • Energetics of the HIV gp120-CD4 binding reaction
    • Myszka, D.G. et al. Energetics of the HIV gp120-CD4 binding reaction. Proc. Natl. Acad. Sci. USA 97, 9026-9031 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9026-9031
    • Myszka, D.G.1
  • 39
    • 56549131177 scopus 로고    scopus 로고
    • The thermodynamics of protein-ligand interaction and solvation: Insights for ligand design
    • Olsson, T.S., Williams, M.A., Pitt, W.R. & Ladbury, J.E. The thermodynamics of protein-ligand interaction and solvation: insights for ligand design. J. Mol. Biol. 384, 1002-1017 (2008).
    • (2008) J. Mol. Biol. , vol.384 , pp. 1002-1017
    • Olsson, T.S.1    Williams, M.A.2    Pitt, W.R.3    Ladbury, J.E.4
  • 40
    • 77956912541 scopus 로고    scopus 로고
    • Protein stability and enzyme activity at extreme biological temperatures
    • Feller, G. Protein stability and enzyme activity at extreme biological temperatures. J. Phys. Condens. Matter 22, 323101 (2010).
    • (2010) J. Phys. Condens. Matter , vol.22 , pp. 323101
    • Feller, G.1
  • 41
    • 4744343045 scopus 로고    scopus 로고
    • Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair
    • Wolf-Watz, M. et al. Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair. Nat. Struct. Mol. Biol. 11, 945-949 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 945-949
    • Wolf-Watz, M.1
  • 42
    • 0034967684 scopus 로고    scopus 로고
    • Early intermediates in the transport cycle of the neuronal excitatory amino acid carrier EAAC1
    • Watzke, N., Bamberg, E. & Grewer, C. Early intermediates in the transport cycle of the neuronal excitatory amino acid carrier EAAC1. J. Gen. Physiol. 117, 547-562 (2001).
    • (2001) J. Gen. Physiol. , vol.117 , pp. 547-562
    • Watzke, N.1    Bamberg, E.2    Grewer, C.3
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4.
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 45
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 46
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M.D., Isupov, M.N. & Murshudov, G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57, 122-133 (2001).
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.