메뉴 건너뛰기




Volumn 44, Issue 24, 2005, Pages 8563-8570

Ligand-protein interaction in biomembrane carriers. The induced transition fit of transport catalysis

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYSIS; GROUND STATE; PROTEINS; SUBSTRATES;

EID: 20544452305     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050543r     Document Type: Article
Times cited : (65)

References (46)
  • 1
    • 0019262972 scopus 로고
    • The utilization of binding energy in coupled vectorial processes
    • Jencks, W. P. (1980) The utilization of binding energy in coupled vectorial processes, Adv. Enzymol. 51, 57-106.
    • (1980) Adv. Enzymol. , vol.51 , pp. 57-106
    • Jencks, W.P.1
  • 2
    • 0001329223 scopus 로고
    • Mechanistic and energetic aspects of carrier catalysis
    • (Kuby, S. A., Ed.) CRC Press, Boca Raton, FL
    • Klingenberg, M. (1991) Mechanistic and energetic aspects of carrier catalysis, in A Study of Enzymes, Volume II: Mechanism of Enzyme Action (Kuby, S. A., Ed.) pp 367-388, CRC Press, Boca Raton, FL.
    • (1991) A Study of Enzymes, Volume II: Mechanism of Enzyme Action , vol.2 , pp. 367-388
    • Klingenberg, M.1
  • 3
    • 0041821836 scopus 로고    scopus 로고
    • A perspective on enzyme catalysis
    • Benkovic, S. J., and Hammes-Schiffer, S. (2003) A perspective on enzyme catalysis, Science 301, 1196-1202.
    • (2003) Science , vol.301 , pp. 1196-1202
    • Benkovic, S.J.1    Hammes-Schiffer, S.2
  • 4
    • 4143115811 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Locher, K. P. (2004) Structure and mechanism of ABC transporters, Curr. Opin. Struct. Biol. 14, 426-431.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 426-431
    • Locher, K.P.1
  • 5
    • 4143072800 scopus 로고    scopus 로고
    • The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily
    • Lemieux, M. J., Huang, Y., and Wang, D. N. (2004) The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily, Curr. Opin. Struct. Biol. 14, 405-412.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 405-412
    • Lemieux, M.J.1    Huang, Y.2    Wang, D.N.3
  • 6
    • 0345307752 scopus 로고    scopus 로고
    • The lactose permease of Escherichia coli: Overall structure, the sugar-binding site and the alternating access model for transport
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Iwata, S., and Kaback, H. R. (2003) The lactose permease of Escherichia coli: Overall structure, the sugar-binding site and the alternating access model for transport, FEBS Lett. 555, 96-101.
    • (2003) FEBS Lett. , vol.555 , pp. 96-101
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Iwata, S.5    Kaback, H.R.6
  • 8
    • 4143061717 scopus 로고    scopus 로고
    • Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: Members of the major facilitator superfamily
    • Abramson, J., Kaback, H. R., and Iwata, S. (2004) Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: Members of the major facilitator superfamily, Curr. Opin. Struct. Biol. 14, 413-419.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 413-419
    • Abramson, J.1    Kaback, H.R.2    Iwata, S.3
  • 9
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool, D., Boudker, O., Jin, Y., and Gouaux, E. (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii, Nature 431, 811-818.
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 10
    • 0141484658 scopus 로고    scopus 로고
    • Projection structure of the atractyloside-inhibited mitochondrial ADP/ATP carrier of Saccharomyces cerevisiae
    • Kunji, E. R., and Harding, M. (2003) Projection structure of the atractyloside-inhibited mitochondrial ADP/ATP carrier of Saccharomyces cerevisiae, J. Biol. Chem. 278, 36985-36988.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36985-36988
    • Kunji, E.R.1    Harding, M.2
  • 12
    • 0016624901 scopus 로고
    • (Meister, A., Ed.) John Wiley & Sons, New York
    • Jencks, W. P. (1975) in Advances in Enzymology (Meister, A., Ed.) Vol. 43, pp 219-410, John Wiley & Sons, New York.
    • (1975) Advances in Enzymology , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 14
    • 9244232678 scopus 로고
    • (Quaglieriello, E., Slater, E. C., Palmieri, F., Saccone, C., and Kroon, A. M., Eds.) Elsevier Science, Amsterdam
    • Klingenberg, M. (1985) in Achievements and Perspectives of Mitochondrial Research. Volume I: Bioenergetics (Quaglieriello, E., Slater, E. C., Palmieri, F., Saccone, C., and Kroon, A. M., Eds.) pp 303-315, Elsevier Science, Amsterdam.
    • (1985) Achievements and Perspectives of Mitochondrial Research. Volume I: Bioenergetics , vol.1 , pp. 303-315
    • Klingenberg, M.1
  • 15
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel, A., and Levitt, M. (1976) Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J. Mol. Biol. 103, 227-249.
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 16
    • 0032500555 scopus 로고    scopus 로고
    • Solvation, reorganization energy, and biological catalysis
    • Cannon, W. R., and Benkovic, S. J. (1998) Solvation, reorganization energy, and biological catalysis, J. Biol. Chem. 273, 26257-26260.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26257-26260
    • Cannon, W.R.1    Benkovic, S.J.2
  • 17
    • 0002449434 scopus 로고
    • The active site and enzyme action
    • Koshland, D. E., Jr. (1960) The active site and enzyme action, Adv. Enzyme Regul. 22, 45-97.
    • (1960) Adv. Enzyme Regul. , vol.22 , pp. 45-97
    • Koshland Jr., D.E.1
  • 18
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen, J., Sharma, S., Quiocho, F. A., and Davidson, A. L. (2001) Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport. Proc. Natl. Acad. Sci. U.S.A. 98, 1525-1530.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 21
    • 0031458238 scopus 로고    scopus 로고
    • Ligand conduction and the gated-pore mechanism of transmembrane transport
    • West, I. C. (1997) Ligand conduction and the gated-pore mechanism of transmembrane transport, Biochim. Biophys. Acta 1331, 213-234.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 213-234
    • West, I.C.1
  • 22
    • 0017657279 scopus 로고
    • Thermodynamics, the structure of integral membrane proteins and transport
    • Singer, S. J. (1977) Thermodynamics, the structure of integral membrane proteins and transport, J. Supramol. Struct. 6, 313-323.
    • (1977) J. Supramol. Struct. , vol.6 , pp. 313-323
    • Singer, S.J.1
  • 23
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. (1966) Simple allosteric model for membrane pumps, Nature 211, 969-970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 25
    • 0001276299 scopus 로고
    • The ADP/ATP shuttle of the mitochondrion
    • Klingenberg, M. (1979) The ADP/ATP shuttle of the mitochondrion, Trends Biochem. Sci. 4, 249-252.
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 249-252
    • Klingenberg, M.1
  • 26
    • 0019875964 scopus 로고
    • Membrane protein oligomeric structure and transport function
    • Klingenberg, M. (1981) Membrane protein oligomeric structure and transport function, Nature 290, 449-454.
    • (1981) Nature , vol.290 , pp. 449-454
    • Klingenberg, M.1
  • 27
    • 0001187696 scopus 로고
    • (Martonosi, A. N., Ed.) Plenum Publishing Corp., New York
    • Klingenberg, M. (1985) in The Enzymes of Biological Membranes (Martonosi, A. N., Ed.) pp 511-553, Plenum Publishing Corp., New York.
    • (1985) The Enzymes of Biological Membranes , pp. 511-553
    • Klingenberg, M.1
  • 28
    • 0343509547 scopus 로고
    • Tracer exchange vs net uptake of glucose through human red cell surface. New evidence for carrier-Mediated diffusion
    • LeFevre, P. G., and McGinniss, G. F. (1960) Tracer Exchange vs Net Uptake of Glucose Through Human Red Cell Surface. New Evidence for Carrier-Mediated Diffusion. J. Gen. Physiol. 44, 87-103.
    • (1960) J. Gen. Physiol. , vol.44 , pp. 87-103
    • Lefevre, P.G.1    McGinniss, G.F.2
  • 30
    • 0020002086 scopus 로고
    • Occlusion of rubidium ions by the sodium-potassium pump: Its implications for the mechanism of potassium transport
    • Glynn, I. M., and Richards, D. E. (1982) Occlusion of rubidium ions by the sodium-potassium pump: Its implications for the mechanism of potassium transport, J. Physiol. 330, 17-43.
    • (1982) J. Physiol. , vol.330 , pp. 17-43
    • Glynn, I.M.1    Richards, D.E.2
  • 31
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sorensen, T. L., Moller, J. V., and Nissen, P. (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump, Science 304, 1672-1675.
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sorensen, T.L.1    Moller, J.V.2    Nissen, P.3
  • 32
    • 0016652192 scopus 로고
    • Evidence for two asymmetric conformational states in the human erythrocyte sugar-transport system
    • Barnett, J. E., Holman, G. D., Chalkley, R. A., and Munday, K. A. (1975) Evidence for two asymmetric conformational states in the human erythrocyte sugar-transport system. Biochem. J. 145, 417-429.
    • (1975) Biochem. J. , vol.145 , pp. 417-429
    • Barnett, J.E.1    Holman, G.D.2    Chalkley, R.A.3    Munday, K.A.4
  • 33
    • 1542664500 scopus 로고
    • (Ernster, L., Estabrook, R. W., and Slater, E. C., Eds.) Elsevier Scientific Publishing Co., Amsterdam
    • Klingenberg, M. (1974) in Dynamics of Energy-Transducing Membranes (Ernster, L., Estabrook, R. W., and Slater, E. C., Eds.) pp 511-528, Elsevier Scientific Publishing Co., Amsterdam.
    • (1974) Dynamics of Energy-Transducing Membranes , pp. 511-528
    • Klingenberg, M.1
  • 34
    • 0014165282 scopus 로고
    • (Nord, F. F., Ed.) Interscience Publishers, New York
    • Mitchell, P. (1967) in Advances in Enzymology (Nord, F. F., Ed.) pp 33-87, Interscience Publishers, New York.
    • (1967) Advances in Enzymology , pp. 33-87
    • Mitchell, P.1
  • 35
    • 0024257073 scopus 로고
    • The phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: Properties, mechanism, and regulation
    • Reizer, J., Saier, M. H., Jr., Deutscher, J., Grenier, F., Thompson, J., and Hengstenberg, W. (1988) The phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: Properties, mechanism, and regulation, Crit. Rev. Microbiol. 15, 297-338.
    • (1988) Crit. Rev. Microbiol. , vol.15 , pp. 297-338
    • Reizer, J.1    Saier Jr., M.H.2    Deutscher, J.3    Grenier, F.4    Thompson, J.5    Hengstenberg, W.6
  • 36
    • 0035979712 scopus 로고    scopus 로고
    • Carbohydrate transporters of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system (PTS)
    • Siebold, C., Flukiger, K., Beutler, R., and Erni, B. (2001) Carbohydrate transporters of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS), FEBS Lett. 504, 104-111.
    • (2001) FEBS Lett. , vol.504 , pp. 104-111
    • Siebold, C.1    Flukiger, K.2    Beutler, R.3    Erni, B.4
  • 37
    • 0019155420 scopus 로고
    • The ADP-ATP translocation in mitochondria, a membrane potential controlled transport
    • Klingenberg, M. (1980) The ADP-ATP Translocation in Mitochondria, a Membrane Potential Controlled Transport, J. Membr. Biol. 56, 97-105.
    • (1980) J. Membr. Biol. , vol.56 , pp. 97-105
    • Klingenberg, M.1
  • 38
    • 0019316929 scopus 로고
    • Reconstitution of adenine nucleotide transport from beef heart mitochondria
    • Krämer, R., and Klingenberg, M. (1980) Reconstitution of adenine nucleotide transport from beef heart mitochondria, Biochemistry 19, 556-560.
    • (1980) Biochemistry , vol.19 , pp. 556-560
    • Krämer, R.1    Klingenberg, M.2
  • 39
    • 0020473267 scopus 로고
    • Electrophorectic control of reconstituted adenine nucleotide translocation
    • Krämer, R., and Klingenberg, M. (1982) Electrophorectic control of reconstituted adenine nucleotide translocation, Biochemistry 21, 1082-1089.
    • (1982) Biochemistry , vol.21 , pp. 1082-1089
    • Krämer, R.1    Klingenberg, M.2
  • 40
    • 0020174563 scopus 로고
    • Temperature dependence of ADP/ATP translocation in mitochondria
    • Klingenberg, M., Grebe, K., and Appel, M. (1982) Temperature Dependence of ADP/ATP Translocation in Mitochondria, Eur. J. Biochem. 126, 263-269.
    • (1982) Eur. J. Biochem. , vol.126 , pp. 263-269
    • Klingenberg, M.1    Grebe, K.2    Appel, M.3
  • 41
    • 0035956859 scopus 로고    scopus 로고
    • The human mitochondrial deoxynucleotide carrier and its role in the toxicity of nucleoside antivirals
    • Dolce, V., Fiermonte, G., Runswick, M. J., Palmieri, F., and Walker, J. E. (2001) The human mitochondrial deoxynucleotide carrier and its role in the toxicity of nucleoside antivirals, Proc. Natl. Acad. Sci. U.S.A. 98, 2284-2288.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2284-2288
    • Dolce, V.1    Fiermonte, G.2    Runswick, M.J.3    Palmieri, F.4    Walker, J.E.5
  • 42
    • 2442650104 scopus 로고    scopus 로고
    • Identification of the mitochondrial GTP/GDP transporter in Saccharomyces cerevisiae
    • Vozza, A., Blanco, E., Palmieri, L., and Palmieri, F. (2004) Identification of the mitochondrial GTP/GDP transporter in Saccharomyces cerevisiae, J. Biol. Chem. 279, 20850-20857.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20850-20857
    • Vozza, A.1    Blanco, E.2    Palmieri, L.3    Palmieri, F.4
  • 44
    • 4344686096 scopus 로고    scopus 로고
    • The yeast peroxisomal adenine nucleotide transporter: Characterization of two transport modes and involvement in ΔpH formation across peroxisomal membranes
    • Lasorsa, F. M., Scarcia, P., Erdmann, R., Palmieri, F., Rottensteiner, H., and Palmieri, L. (2004) The yeast peroxisomal adenine nucleotide transporter: Characterization of two transport modes and involvement in ΔpH formation across peroxisomal membranes, Biochem. J. 381, 581-585.
    • (2004) Biochem. J. , vol.381 , pp. 581-585
    • Lasorsa, F.M.1    Scarcia, P.2    Erdmann, R.3    Palmieri, F.4    Rottensteiner, H.5    Palmieri, L.6
  • 45
    • 0032901360 scopus 로고    scopus 로고
    • Structure and function of the uncoupling protein from brown adipose tissue
    • Klingenberg, M., and Huang, S. G. (1999) Structure and function of the uncoupling protein from brown adipose tissue, Biochim. Biophys. Acta 1415, 271-296.
    • (1999) Biochim. Biophys. Acta , vol.1415 , pp. 271-296
    • Klingenberg, M.1    Huang, S.G.2
  • 46
    • 0022273195 scopus 로고
    • Principles of carrier catalysis elucidated by comparing two similar membrane translocators from mitochondria, the ADP/ATP carrier and the uncoupling protein
    • Klingenberg, M. (1985) Principles of carrier catalysis elucidated by comparing two similar membrane translocators from mitochondria, the ADP/ATP carrier and the uncoupling protein, Ann. N.Y. Acad. Sci. 456, 279-288.
    • (1985) Ann. N.Y. Acad. Sci. , vol.456 , pp. 279-288
    • Klingenberg, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.