메뉴 건너뛰기




Volumn 92, Issue 10, 2007, Pages 3474-3491

Lactose permease H+-lactose symporter: Mechanical switch or Brownian ratchet?

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARTIC ACID; CARBOHYDRATE DERIVATIVE; COTRANSPORTER; DOCKING PROTEIN; GALACTOSE; GLUTAMIC ACID; IMIDAZOLE DERIVATIVE; LACTOSE PERMEASE; LYSINE; MELIBIOSE; PROTON;

EID: 34248194465     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.100669     Document Type: Article
Times cited : (18)

References (100)
  • 1
    • 4444328639 scopus 로고    scopus 로고
    • Lactose permease as a paradigm for membrane transport proteins (Review)
    • Abramson, J., S. Iwata, and H. R. Kaback. 2004. Lactose permease as a paradigm for membrane transport proteins (Review). Mol. Membr. Biol. 21:227-236.
    • (2004) Mol. Membr. Biol , vol.21 , pp. 227-236
    • Abramson, J.1    Iwata, S.2    Kaback, H.R.3
  • 2
    • 4143061717 scopus 로고    scopus 로고
    • Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: Members of the major facilitator superfamily
    • Abramson, J., H. R. Kaback, and S. Iwata. 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
  • 3
    • 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., I. Smirnova, V. Kasho, G. Verner, S. Iwata, and H. R. Kaback. 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
  • 4
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., I. Smirnova, V. Kasho, G. Verner, H. R. Kaback, and S. Iwata. 2003. Structure and mechanism of the lactose permease of Escherichia coli. Science. 301:610-615.
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 5
    • 0037076369 scopus 로고    scopus 로고
    • Changing the lactose permease of Escherichia coli into a galactose-specific symporter
    • Guan, L., M. Sahin-Toth, and H. R. Kaback. 2002. Changing the lactose permease of Escherichia coli into a galactose-specific symporter. Proc. Natl. Acad. Sci. USA. 99:6613-6618.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6613-6618
    • Guan, L.1    Sahin-Toth, M.2    Kaback, H.R.3
  • 6
    • 0038212926 scopus 로고    scopus 로고
    • Ligand recognition by the lactose permease of Escherichia coli: Specificity and affinity are defined by distinct structural elements of galactopyranosides
    • Sahin-Toth, M., K. M. Akhoon, J. Runner, and H. R. Kaback. 2000. Ligand recognition by the lactose permease of Escherichia coli: specificity and affinity are defined by distinct structural elements of galactopyranosides. Biochemistry. 39:5097-5103.
    • (2000) Biochemistry , vol.39 , pp. 5097-5103
    • Sahin-Toth, M.1    Akhoon, K.M.2    Runner, J.3    Kaback, H.R.4
  • 7
    • 33645320817 scopus 로고    scopus 로고
    • Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY
    • Mirza, O., L. Guan, G. Verner, S. Iwata, and H. R. Kaback. 2006. Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY. EMBO J. 25:1177-1183.
    • (2006) EMBO J , vol.25 , pp. 1177-1183
    • Mirza, O.1    Guan, L.2    Verner, G.3    Iwata, S.4    Kaback, H.R.5
  • 8
    • 0035823221 scopus 로고    scopus 로고
    • Helix packing in the lactose permease of Escherichia coli: Localization of helix VI
    • Guan, L., A. B. Weinglass, and H. R. Kaback. 2001. Helix packing in the lactose permease of Escherichia coli: localization of helix VI. J. Mol. Biol. 312:69-77.
    • (2001) J. Mol. Biol , vol.312 , pp. 69-77
    • Guan, L.1    Weinglass, A.B.2    Kaback, H.R.3
  • 9
    • 0025260988 scopus 로고
    • Characterization of the double mutant, Val-177/Asn-322, of the lactose permease
    • Brooker, R. J. 1990. Characterization of the double mutant, Val-177/Asn-322, of the lactose permease. J. Biol. Chem. 265:4155-4160.
    • (1990) J. Biol. Chem , vol.265 , pp. 4155-4160
    • Brooker, R.J.1
  • 10
    • 0024506444 scopus 로고
    • Galactoside-dependent proton transport by mutants of the Escherichia coli lactose carrier. Replacement of histidine 322 by tyrosine or phenylalanine
    • King, S. C., and T. H. Wilson. 1989. Galactoside-dependent proton transport by mutants of the Escherichia coli lactose carrier. Replacement of histidine 322 by tyrosine or phenylalanine. J. Biol. Chem. 264:7390-7394.
    • (1989) J. Biol. Chem , vol.264 , pp. 7390-7394
    • King, S.C.1    Wilson, T.H.2
  • 11
    • 0030054158 scopus 로고    scopus 로고
    • Physiological evidence for an interaction between Glu-325 and His-322 in the lactose carrier of Escherichia coli
    • Lee, J. I., M. F. Varela, and T. H. Wilson. 1996. Physiological evidence for an interaction between Glu-325 and His-322 in the lactose carrier of Escherichia coli. Biochim. Biophys. Acta. 1278:111-118.
    • (1996) Biochim. Biophys. Acta , vol.1278 , pp. 111-118
    • Lee, J.I.1    Varela, M.F.2    Wilson, T.H.3
  • 12
    • 0023047653 scopus 로고
    • lac permease of Escherichia coli: Histidine-205 and histidine-322 play different roles in lactose/H+ symport
    • Puttner, I. B., H. K. Sarkar, M. S. Poonian, and H. R. Kaback. 1986. lac permease of Escherichia coli: histidine-205 and histidine-322 play different roles in lactose/H+ symport. Biochemistry. 25:4483-4485.
    • (1986) Biochemistry , vol.25 , pp. 4483-4485
    • Puttner, I.B.1    Sarkar, H.K.2    Poonian, M.S.3    Kaback, H.R.4
  • 13
    • 0033548256 scopus 로고    scopus 로고
    • A K319N/E325Q double mutant of the lactose permease cotransports H+ with lactose. Implications for a proposed mechanism of H+/lactose symport
    • Johnson, J. L., and R. J. Brooker. 1999. A K319N/E325Q double mutant of the lactose permease cotransports H+ with lactose. Implications for a proposed mechanism of H+/lactose symport. J. Biol. Chem. 274:4074-4081.
    • (1999) J. Biol. Chem , vol.274 , pp. 4074-4081
    • Johnson, J.L.1    Brooker, R.J.2
  • 14
    • 33845380397 scopus 로고    scopus 로고
    • Sugar binding and protein conformational changes in lactose permease
    • Yin, Y., M. O. Jensen, E. Tajkhorshid, and K. Schulten. 2006. Sugar binding and protein conformational changes in lactose permease. Biophys. J. 91:3972-3985.
    • (2006) Biophys. J , vol.91 , pp. 3972-3985
    • Yin, Y.1    Jensen, M.O.2    Tajkhorshid, E.3    Schulten, K.4
  • 15
    • 33750454136 scopus 로고    scopus 로고
    • AsSuppressor analysis of residues involved in cation transport in the lactose permease: Identification of a coupling sensor
    • Franco, P. J., E. A. Matzke, J. L. Johnson, B. M. Wiczer, and R. J. Brooker. 2006. AsSuppressor analysis of residues involved in cation transport in the lactose permease: identification of a coupling sensor. J. Membr. Biol. 211:101-113.
    • (2006) J. Membr. Biol , vol.211 , pp. 101-113
    • Franco, P.J.1    Matzke, E.A.2    Johnson, J.L.3    Wiczer, B.M.4    Brooker, R.J.5
  • 16
    • 0026757193 scopus 로고
    • Possible salt bridges between transmembrane α-helices of the lactose carrier of Escherichia coli
    • Lee, J. I., P. P. Hwang, C. Hansen, and T. H. Wilson. 1992. Possible salt bridges between transmembrane α-helices of the lactose carrier of Escherichia coli. J. Biol. Chem. 267:20758-20764.
    • (1992) J. Biol. Chem , vol.267 , pp. 20758-20764
    • Lee, J.I.1    Hwang, P.P.2    Hansen, C.3    Wilson, T.H.4
  • 17
    • 0026087282 scopus 로고
    • The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of Escherichia coli
    • King, S. C., C. L. Hansen, and T. H. Wilson. 1991. The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of Escherichia coli. Biochim. Biophys. Acta. 1062:177-186.
    • (1991) Biochim. Biophys. Acta , vol.1062 , pp. 177-186
    • King, S.C.1    Hansen, C.L.2    Wilson, T.H.3
  • 18
    • 0026439214 scopus 로고
    • Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli
    • Sahin-Toth, M., R. L. Dunten, A. Gonzalez, and H. R. Kaback. 1992. Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. USA. 89:10547-10551.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10547-10551
    • Sahin-Toth, M.1    Dunten, R.L.2    Gonzalez, A.3    Kaback, H.R.4
  • 19
    • 0034718616 scopus 로고    scopus 로고
    • Unraveling the mechanism of the lactose permease of Escherichia coli
    • Sahin-Toth, M., A. Karlin, and H. R. Kaback. 2000. Unraveling the mechanism of the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. USA. 97:10729-10732.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10729-10732
    • Sahin-Toth, M.1    Karlin, A.2    Kaback, H.R.3
  • 21
    • 0025324528 scopus 로고
    • Identification of valine 177 as a mutation altering specificity for transport of sugars by the Escherichia coli lactose carrier. Enhanced specificity for sucrose and maltose
    • King, S. C., and T. H. Wilson. 1990. Identification of valine 177 as a mutation altering specificity for transport of sugars by the Escherichia coli lactose carrier. Enhanced specificity for sucrose and maltose. J. Biol. Chem. 265:9638-9644.
    • (1990) J. Biol. Chem , vol.265 , pp. 9638-9644
    • King, S.C.1    Wilson, T.H.2
  • 22
    • 0025759935 scopus 로고
    • Kinetic analysis of lactose exchange in proteoliposomes reconstituted with purified lac permease
    • Lolkema, J. S., N. Carrasco, and H. R. Kaback. 1991. Kinetic analysis of lactose exchange in proteoliposomes reconstituted with purified lac permease. Biochemistry. 30:1284-1290.
    • (1991) Biochemistry , vol.30 , pp. 1284-1290
    • Lolkema, J.S.1    Carrasco, N.2    Kaback, H.R.3
  • 23
    • 0029013235 scopus 로고
    • Uncoupling in secondary transport proteins. A mechanistic explanation for mutants of lac permease with an uncoupled phenotype
    • Lolkema, J. S., and B. Poolman. 1995. Uncoupling in secondary transport proteins. A mechanistic explanation for mutants of lac permease with an uncoupled phenotype. J. Biol. Chem. 270:12670-12676.
    • (1995) J. Biol. Chem , vol.270 , pp. 12670-12676
    • Lolkema, J.S.1    Poolman, B.2
  • 24
    • 0018380688 scopus 로고
    • Lactose carrier protein of Escherichia coli. Transport and binding of 2′-(N-dansyl)aminoethyl β-D-thiogalactopyranoside and p-nitrophenyl α-d-galactopyranoside
    • Overath, P., R. M. Teather, R. D. Simoni, G. Aichele, and U. Wilhelm. 1979. Lactose carrier protein of Escherichia coli. Transport and binding of 2′-(N-dansyl)aminoethyl β-D-thiogalactopyranoside and p-nitrophenyl α-d-galactopyranoside. Biochemistry. 18:1-11.
    • (1979) Biochemistry , vol.18 , pp. 1-11
    • Overath, P.1    Teather, R.M.2    Simoni, R.D.3    Aichele, G.4    Wilhelm, U.5
  • 25
    • 0019159620 scopus 로고
    • Kinetics of lactose transport into Escherichia coli in the presence and absence of a protonmotive force
    • Page, M. G., and I. C. West. 1980. Kinetics of lactose transport into Escherichia coli in the presence and absence of a protonmotive force. FEBS Lett. 120:187-191.
    • (1980) FEBS Lett , vol.120 , pp. 187-191
    • Page, M.G.1    West, I.C.2
  • 26
    • 0019410993 scopus 로고
    • The kinetics of the β-galactosideproton symport of Escherichia coli
    • Page, M. G., and I. C. West. 1981. The kinetics of the β-galactosideproton symport of Escherichia coli. Biochem. J. 196:721-731.
    • (1981) Biochem. J , vol.196 , pp. 721-731
    • Page, M.G.1    West, I.C.2
  • 27
    • 0026802129 scopus 로고
    • Lactose transport system of Streptococcus thermophilus. The role of histidine residues
    • Poolman, B., R. Modderman, and J. Reizer. 1992. Lactose transport system of Streptococcus thermophilus. The role of histidine residues. J. Biol. Chem. 267:9150-9157.
    • (1992) J. Biol. Chem , vol.267 , pp. 9150-9157
    • Poolman, B.1    Modderman, R.2    Reizer, J.3
  • 28
    • 4344647988 scopus 로고    scopus 로고
    • Binding affinity of lactose permease is not altered by the H+ electrochemical gradient
    • Guan, L., and H. R. Kaback. 2004. Binding affinity of lactose permease is not altered by the H+ electrochemical gradient. Proc. Natl. Acad. Sci. USA. 101:12148-12152.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12148-12152
    • Guan, L.1    Kaback, H.R.2
  • 29
    • 0018408688 scopus 로고
    • Evidence of multiple operational affinities for D-glucose inside the human erythrocyte membrane
    • Baker, G. F., and R. J. Naftalin. 1979. Evidence of multiple operational affinities for D-glucose inside the human erythrocyte membrane. Biochim. Biophys. Acta. 550:474-484.
    • (1979) Biochim. Biophys. Acta , vol.550 , pp. 474-484
    • Baker, G.F.1    Naftalin, R.J.2
  • 30
    • 33646836322 scopus 로고    scopus 로고
    • Docking studies show that D-glucose and quercetin slide through the transporter GLUT1
    • Cunningham, P., I. Afzal-Ahmed, and R. J. Naftalin. 2006. Docking studies show that D-glucose and quercetin slide through the transporter GLUT1. J. Biol. Chem. 281:5797-5803.
    • (2006) J. Biol. Chem , vol.281 , pp. 5797-5803
    • Cunningham, P.1    Afzal-Ahmed, I.2    Naftalin, R.J.3
  • 31
    • 0033593017 scopus 로고    scopus 로고
    • The human erythrocyte sugar transporter presents two sugar import sites
    • Hamill, S., E. K. Cloherty, and A. Carruthers. 1999. The human erythrocyte sugar transporter presents two sugar import sites. Biochemistry. 38:16974-16983.
    • (1999) Biochemistry , vol.38 , pp. 16974-16983
    • Hamill, S.1    Cloherty, E.K.2    Carruthers, A.3
  • 32
    • 0037159240 scopus 로고    scopus 로고
    • Molecular determinants of sugar transport regulation by ATP
    • Levine, K. B., E. K. Cloherty, S. Hamill, and A. Carruthers. 2002. Molecular determinants of sugar transport regulation by ATP. Biochemistry. 41:12629-12638.
    • (2002) Biochemistry , vol.41 , pp. 12629-12638
    • Levine, K.B.1    Cloherty, E.K.2    Hamill, S.3    Carruthers, A.4
  • 33
    • 0025861986 scopus 로고
    • Evidence that the asparagine 322 mutant of the lactose permease transports protons and lactose with a normal stoichiometry and accumulates lactose against a concentration gradient
    • Franco, P. J., and R. J. Brooker. 1991. Evidence that the asparagine 322 mutant of the lactose permease transports protons and lactose with a normal stoichiometry and accumulates lactose against a concentration gradient. J. Biol. Chem. 266:6693-6699.
    • (1991) J. Biol. Chem , vol.266 , pp. 6693-6699
    • Franco, P.J.1    Brooker, R.J.2
  • 34
    • 0025290251 scopus 로고
    • Characterization of Escherichia coli lactose carrier mutants that transport protons without a cosubstrate. Probes for the energy barrier to uncoupled transport
    • King, S. C., and T. H. Wilson. 1990. Characterization of Escherichia coli lactose carrier mutants that transport protons without a cosubstrate. Probes for the energy barrier to uncoupled transport. J. Biol. Chem. 265:9645-9651.
    • (1990) J. Biol. Chem , vol.265 , pp. 9645-9651
    • King, S.C.1    Wilson, T.H.2
  • 35
    • 0025259658 scopus 로고
    • Sensitivity of efflux-driven carrier turnover to external pH in mutants of the Escherichia coli lactose carrier that have tyrosine or phenylalanine substituted for histidine-322. A comparison of lactose and melibiose
    • King, S. C., and T. H. Wilson. 1990. Sensitivity of efflux-driven carrier turnover to external pH in mutants of the Escherichia coli lactose carrier that have tyrosine or phenylalanine substituted for histidine-322. A comparison of lactose and melibiose. J. Biol. Chem. 265:3153-3160.
    • (1990) J. Biol. Chem , vol.265 , pp. 3153-3160
    • King, S.C.1    Wilson, T.H.2
  • 36
    • 0029044257 scopus 로고
    • Kinetic analysis of lactose and proton coupling in Glu379 mutants of the lactose transport protein of Streptococcus thermophilus
    • Poolman, B., J. Knol, and J. S. Lolkema. 1995. Kinetic analysis of lactose and proton coupling in Glu379 mutants of the lactose transport protein of Streptococcus thermophilus. J. Biol. Chem. 270:12995-13003.
    • (1995) J. Biol. Chem , vol.270 , pp. 12995-13003
    • Poolman, B.1    Knol, J.2    Lolkema, J.S.3
  • 37
    • 0024497110 scopus 로고
    • Fast measurement of galactoside transport by lactose permease
    • Dornmair, K., P. Overath, and F. Jahnig. 1989. Fast measurement of galactoside transport by lactose permease. J. Biol. Chem. 264:342-346.
    • (1989) J. Biol. Chem , vol.264 , pp. 342-346
    • Dornmair, K.1    Overath, P.2    Jahnig, F.3
  • 38
    • 0021378172 scopus 로고
    • Purification of the lactose:H+ carrier of Escherichia coli and characterization of galactoside binding and transport
    • Wright, J. K., and P. Overath. 1984. Purification of the lactose:H+ carrier of Escherichia coli and characterization of galactoside binding and transport. Eur. J. Biochem. 138:497-508.
    • (1984) Eur. J. Biochem , vol.138 , pp. 497-508
    • Wright, J.K.1    Overath, P.2
  • 39
    • 0035112524 scopus 로고    scopus 로고
    • Time-resolved study of the inner space of lactose permease
    • Nachliel, E., N. Pollak, D. Huppert, and M. Gutman. 2001. Time-resolved study of the inner space of lactose permease. Biophys. J. 80:1498-1506.
    • (2001) Biophys. J , vol.80 , pp. 1498-1506
    • Nachliel, E.1    Pollak, N.2    Huppert, D.3    Gutman, M.4
  • 40
    • 0035801845 scopus 로고    scopus 로고
    • Probing of the substrate binding domain of lactose permease by a proton pulse
    • Nachliel, E., and M. Gutman. 2001. Probing of the substrate binding domain of lactose permease by a proton pulse. Biochim. Biophys. Acta. 1514:33-50.
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 33-50
    • Nachliel, E.1    Gutman, M.2
  • 41
    • 2642541140 scopus 로고    scopus 로고
    • Control of H+/lactose coupling by ionic interactions in the lactose permease of Escherichia coli
    • Johnson, J. L., and R. J. Brooker. 2004. Control of H+/lactose coupling by ionic interactions in the lactose permease of Escherichia coli. J. Membr. Biol. 198:135-146.
    • (2004) J. Membr. Biol , vol.198 , pp. 135-146
    • Johnson, J.L.1    Brooker, R.J.2
  • 42
    • 0025765577 scopus 로고
    • An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. II. Second site revertants of the thiodigalactoside-dependent proton leak by the Val177/Asn319 permease
    • Eelkema, J. A., M. A. O'Donnell, and R. J. Brooker. 1991. An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. II. Second site revertants of the thiodigalactoside-dependent proton leak by the Val177/Asn319 permease. J. Biol. Chem. 266:4139-4144.
    • (1991) J. Biol. Chem , vol.266 , pp. 4139-4144
    • Eelkema, J.A.1    O'Donnell, M.A.2    Brooker, R.J.3
  • 43
    • 0026760611 scopus 로고
    • Amino acid substitution in the lactose carrier protein with the use of amber suppressors
    • Huang, A. M., J. I. Lee, S. C. King, and T. H. Wilson. 1992. Amino acid substitution in the lactose carrier protein with the use of amber suppressors. J. Bacteriol. 174:5436-5441.
    • (1992) J. Bacteriol , vol.174 , pp. 5436-5441
    • Huang, A.M.1    Lee, J.I.2    King, S.C.3    Wilson, T.H.4
  • 44
    • 0025057345 scopus 로고
    • Mechanism of enhanced melibiose transport rate catalyzed by an Escherichia coli lactose carrier mutant with leucine substituted for serine-306. The pH-dependence of melibiose efflux
    • King, S. C., and T. H.Wilson. 1990. Mechanism of enhanced melibiose transport rate catalyzed by an Escherichia coli lactose carrier mutant with leucine substituted for serine-306. The pH-dependence of melibiose efflux. Biochim. Biophys. Acta. 1022:373-380.
    • (1990) Biochim. Biophys. Acta , vol.1022 , pp. 373-380
    • King, S.C.1    Wilson, T.H.2
  • 45
    • 0030924137 scopus 로고    scopus 로고
    • Lactose carrier mutants of Escherichia coli with changes in sugar recognition (lactose versus melibiose)
    • Varela, M. F., R. J. Brooker, and T. H. Wilson. 1997. Lactose carrier mutants of Escherichia coli with changes in sugar recognition (lactose versus melibiose). J. Bacteriol. 179:5570-5573.
    • (1997) J. Bacteriol , vol.179 , pp. 5570-5573
    • Varela, M.F.1    Brooker, R.J.2    Wilson, T.H.3
  • 46
    • 0028007043 scopus 로고
    • Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 2. Site-directed fluorescence studies
    • Wu, J., and H. R. Kaback. 1994. Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 2. Site-directed fluorescence studies. Biochemistry. 33:12166-12171.
    • (1994) Biochemistry , vol.33 , pp. 12166-12171
    • Wu, J.1    Kaback, H.R.2
  • 47
    • 0030203710 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4
    • Morris, G. M., D. S. Goodsell, R. Huey, and A. J. Olson. 1996. Distributed automated docking of flexible ligands to proteins: parallel applications of AutoDock 2.4. J. Comput. Aided Mol. Des. 10:293-304.
    • (1996) J. Comput. Aided Mol. Des , vol.10 , pp. 293-304
    • Morris, G.M.1    Goodsell, D.S.2    Huey, R.3    Olson, A.J.4
  • 48
    • 0025831225 scopus 로고
    • An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. I. Val177 and Val177/Asn319 permeases facilitate proton uniport and sugar uniport
    • Brooker, R. J. 1991. An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. I. Val177 and Val177/Asn319 permeases facilitate proton uniport and sugar uniport. J. Biol. Chem. 266:4131-4138.
    • (1991) J. Biol. Chem , vol.266 , pp. 4131-4138
    • Brooker, R.J.1
  • 49
    • 0027454507 scopus 로고
    • Lactose permease mutants which transport (malto)-oligosaccharides
    • Olsen, S. G., K. M. Greene, and R. J. Brooker. 1993. Lactose permease mutants which transport (malto)-oligosaccharides. J. Bacteriol. 175:6269-6275.
    • (1993) J. Bacteriol , vol.175 , pp. 6269-6275
    • Olsen, S.G.1    Greene, K.M.2    Brooker, R.J.3
  • 50
    • 12344321851 scopus 로고    scopus 로고
    • Predicting the three-dimensional structure of the human facilitative glucose transporter glut1 by a novel evolutionary homology strategy: Insights on the molecular mechanism of substrate migration, and binding sites for glucose and inhibitory molecules
    • Salas-Burgos, A., P. Iserovich, F. Zuniga, J. C. Vera, and J. Fischbarg. 2004. Predicting the three-dimensional structure of the human facilitative glucose transporter glut1 by a novel evolutionary homology strategy: insights on the molecular mechanism of substrate migration, and binding sites for glucose and inhibitory molecules. Biophys. J. 87:2990-2999.
    • (2004) Biophys. J , vol.87 , pp. 2990-2999
    • Salas-Burgos, A.1    Iserovich, P.2    Zuniga, F.3    Vera, J.C.4    Fischbarg, J.5
  • 51
    • 33845945208 scopus 로고    scopus 로고
    • Direct sugar binding to LacY measured by resonance energy transfer
    • Smirnova, I. N., V. N. Kasho, and H. R. Kaback. 2006. Direct sugar binding to LacY measured by resonance energy transfer. Biochemistry. 45:15279-15287.
    • (2006) Biochemistry , vol.45 , pp. 15279-15287
    • Smirnova, I.N.1    Kasho, V.N.2    Kaback, H.R.3
  • 52
    • 33751248521 scopus 로고    scopus 로고
    • Modeling, docking, and simulation of the major facilitator superfamily
    • Holyoake, J., V. Caulfield, S. A. Baldwin, and M. S. Sansom. 2006. Modeling, docking, and simulation of the major facilitator superfamily. Biophys. J. 91:L84-L86.
    • (2006) Biophys. J , vol.91
    • Holyoake, J.1    Caulfield, V.2    Baldwin, S.A.3    Sansom, M.S.4
  • 53
    • 33646343221 scopus 로고    scopus 로고
    • Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): A mechanism of electron transfer and proton conduction during ubiquinone reduction
    • Horsefield, R., V. Yankovskaya, G. Sexton, W. Whittingham, K. Shiomi, S. Omura, B. Byrne, G. Cecchini, and S. Iwata. 2006. Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction. J. Biol. Chem. 281:7309-7316.
    • (2006) J. Biol. Chem , vol.281 , pp. 7309-7316
    • Horsefield, R.1    Yankovskaya, V.2    Sexton, G.3    Whittingham, W.4    Shiomi, K.5    Omura, S.6    Byrne, B.7    Cecchini, G.8    Iwata, S.9
  • 54
    • 33947481318 scopus 로고
    • Quantitative Raman spectroscopy for determination of base strengths of weak organic bases
    • Deno, N. C., and M. J. Wisotsky. 1963. Quantitative Raman spectroscopy for determination of base strengths of weak organic bases. J. Am. Chem. Soc. 85:1735-1736.
    • (1963) J. Am. Chem. Soc , vol.85 , pp. 1735-1736
    • Deno, N.C.1    Wisotsky, M.J.2
  • 55
    • 0000329487 scopus 로고
    • Basicity of alcohols and ethers
    • Deno, N. C., and J. O. Turner. 1966. Basicity of alcohols and ethers. J. Org. Chem. 31:1969.
    • (1966) J. Org. Chem , vol.31 , pp. 1969
    • Deno, N.C.1    Turner, J.O.2
  • 56
    • 0344278782 scopus 로고
    • NMR study of the protolysis kinetics in methanol and ethanol
    • **
    • Luz, Z., D. Gill, and S. Meiboom. 1959. NMR study of the protolysis kinetics in methanol and ethanol. J. Chem. Phys. 30:1540-1545.**
    • (1959) J. Chem. Phys , vol.30 , pp. 1540-1545
    • Luz, Z.1    Gill, D.2    Meiboom, S.3
  • 57
    • 0001167471 scopus 로고
    • Fast reactions of imidazole studied with relaxation spectrometry
    • Eigen, M., G. G. Hammes, and K. Kustin. 1960. Fast reactions of imidazole studied with relaxation spectrometry. J. Am. Chem. Soc. 82:3482-3483.
    • (1960) J. Am. Chem. Soc , vol.82 , pp. 3482-3483
    • Eigen, M.1    Hammes, G.G.2    Kustin, K.3
  • 58
    • 0039789834 scopus 로고
    • Elementary steps in enzyme reactions (as studies by relaxation spectrometry)
    • Eigen, M., and G. G. Hammes. 1963. Elementary steps in enzyme reactions (as studies by relaxation spectrometry). Adv. Enzymol. Relat. Subj. Biochem. 25:1-38.
    • (1963) Adv. Enzymol. Relat. Subj. Biochem , vol.25 , pp. 1-38
    • Eigen, M.1    Hammes, G.G.2
  • 59
    • 33846511701 scopus 로고    scopus 로고
    • Comparative (1)H NMR and molecular modeling study of hydroxy protons of beta-d-Galp-(1→4)-beta-d-GlcpNAc-(1→2)-alpha-d- Manp-(1→O)(CH(2)(7)C H(3) analogues in aqueous solution
    • Rohfritsch, P. F., M. Frank, C. Sandstrom, L. Kenne, J. F. Vliegenthart, and J. P. Kamerling. 2006. Comparative (1)H NMR and molecular modeling study of hydroxy protons of beta-d-Galp-(1→4)-beta-d-GlcpNAc-(1→2)-alpha-d- Manp-(1→O)(CH(2)(7)C H(3) analogues in aqueous solution. Carbohydr. Res. 342:597-609.
    • (2006) Carbohydr. Res , vol.342 , pp. 597-609
    • Rohfritsch, P.F.1    Frank, M.2    Sandstrom, C.3    Kenne, L.4    Vliegenthart, J.F.5    Kamerling, J.P.6
  • 60
    • 0025424768 scopus 로고
    • New developments in biochemical mass spectrometry: Electrospray ionization
    • Smith, R. D., J. A. Loo, C. G. Edmonds, C. J. Barinaga, and H. R. Udseth. 1990. New developments in biochemical mass spectrometry: electrospray ionization. Anal. Chem. 62:882-899.
    • (1990) Anal. Chem , vol.62 , pp. 882-899
    • Smith, R.D.1    Loo, J.A.2    Edmonds, C.G.3    Barinaga, C.J.4    Udseth, H.R.5
  • 62
    • 33645453945 scopus 로고    scopus 로고
    • Beyond switches: Ratcheting a particle energetically uphill with a compart-mentalized molecular machine
    • Chatterjee, M. N., E. R. Kay, and D. A. Leigh. 2006. Beyond switches: ratcheting a particle energetically uphill with a compart-mentalized molecular machine. J. Am. Chem. Soc. 128:4058-4073.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 4058-4073
    • Chatterjee, M.N.1    Kay, E.R.2    Leigh, D.A.3
  • 63
    • 9444256373 scopus 로고    scopus 로고
    • A reversible synthetic rotary molecular motor
    • Hernandez, J. V., E. R. Kay, and D. A. Leigh. 2004. A reversible synthetic rotary molecular motor. Science. 306:1532-1537.
    • (2004) Science , vol.306 , pp. 1532-1537
    • Hernandez, J.V.1    Kay, E.R.2    Leigh, D.A.3
  • 64
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • DeCoursey, T. E. 2003. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:475-579.
    • (2003) Physiol. Rev , vol.83 , pp. 475-579
    • DeCoursey, T.E.1
  • 65
    • 34248138636 scopus 로고
    • Generation of Coulomb wave functions by means of recurrence relations
    • Stegun, I. A., and M. Abramowitz. 1955. Generation of Coulomb wave functions by means of recurrence relations. Phys. Rev. 98:1851-1852.
    • (1955) Phys. Rev , vol.98 , pp. 1851-1852
    • Stegun, I.A.1    Abramowitz, M.2
  • 66
    • 0028234751 scopus 로고
    • Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli
    • Franco, P. J., and R. J. Brooker. 1994. Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli. J. Biol. Chem. 269:7379-7386.
    • (1994) J. Biol. Chem , vol.269 , pp. 7379-7386
    • Franco, P.J.1    Brooker, R.J.2
  • 67
    • 0035932954 scopus 로고    scopus 로고
    • Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichiacoli
    • Sahin-Toth, M., and H. R. Kaback. 2001. Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichiacoli. Proc. Natl. Acad. Sci. USA. 98:6068-6073.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6068-6073
    • Sahin-Toth, M.1    Kaback, H.R.2
  • 68
    • 0028313224 scopus 로고
    • Role of glutamate-269 in the lactose permease of Escherichia coli
    • Ujwal, M. L., M. Sahin-Toth, B. Persson, and H. R. Kaback. 1994. Role of glutamate-269 in the lactose permease of Escherichia coli. Mol. Membr. Biol. 11:9-16.
    • (1994) Mol. Membr. Biol , vol.11 , pp. 9-16
    • Ujwal, M.L.1    Sahin-Toth, M.2    Persson, B.3    Kaback, H.R.4
  • 70
    • 0027203537 scopus 로고
    • Lysine 319 interacts with both glutamic acid 269 and aspartic acid 240 in the lactose carrier of Escherichia coli
    • Lee, J. I., P. P. Hwang, and T. H. Wilson. 1993. Lysine 319 interacts with both glutamic acid 269 and aspartic acid 240 in the lactose carrier of Escherichia coli. J. Biol. Chem. 268:20007-20015.
    • (1993) J. Biol. Chem , vol.268 , pp. 20007-20015
    • Lee, J.I.1    Hwang, P.P.2    Wilson, T.H.3
  • 71
    • 0027382884 scopus 로고
    • Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli
    • Sahin-Toth, M., and H. R. Kaback. 1993. Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli. Biochemistry. 32:10027-10035.
    • (1993) Biochemistry , vol.32 , pp. 10027-10035
    • Sahin-Toth, M.1    Kaback, H.R.2
  • 72
    • 0027419744 scopus 로고
    • Role of the charge pair aspartic acid-237-lysine-358 in the lactose permease of Escherichia coli
    • Dunten, R. L., M. Sahin-Toth, and H. R. Kaback. 1993. Role of the charge pair aspartic acid-237-lysine-358 in the lactose permease of Escherichia coli. Biochemistry. 32:3139-3145.
    • (1993) Biochemistry , vol.32 , pp. 3139-3145
    • Dunten, R.L.1    Sahin-Toth, M.2    Kaback, H.R.3
  • 73
    • 0024583550 scopus 로고
    • Characterization of site-directed mutants in the lac permease of Escherichia coli. Replacement of histidine residues
    • Puttner, I. B., H. K. Sarkar, E. Padan, J. S. Lolkema, and H. R. Kaback. 1989. Characterization of site-directed mutants in the lac permease of Escherichia coli. Replacement of histidine residues. Biochemistry. 28:2525-2533.
    • (1989) Biochemistry , vol.28 , pp. 2525-2533
    • Puttner, I.B.1    Sarkar, H.K.2    Padan, E.3    Lolkema, J.S.4    Kaback, H.R.5
  • 74
    • 0023047638 scopus 로고
    • lac permease of Escherichia coli: Histidine-322 and glutamic acid-325 may be components of a charge-relay system
    • Carrasco, N., L. M. Antes, M. S. Poonian, and H. R. Kaback. 1986. lac permease of Escherichia coli: histidine-322 and glutamic acid-325 may be components of a charge-relay system. Biochemistry. 25:4486-4488.
    • (1986) Biochemistry , vol.25 , pp. 4486-4488
    • Carrasco, N.1    Antes, L.M.2    Poonian, M.S.3    Kaback, H.R.4
  • 75
    • 0024535468 scopus 로고
    • Effect of distance and orientation between arginine-302, histidine-322, and glutamate-325 on the activity of lac permease from Escherichia coli
    • Lee, J. A., I. B. Puttner, and H. R. Kaback. 1989. Effect of distance and orientation between arginine-302, histidine-322, and glutamate-325 on the activity of lac permease from Escherichia coli. Biochemistry. 28:2540-2544.
    • (1989) Biochemistry , vol.28 , pp. 2540-2544
    • Lee, J.A.1    Puttner, I.B.2    Kaback, H.R.3
  • 76
    • 0023974393 scopus 로고
    • lac permease of Escherichia coli containing a single histidine residue is fully functional
    • Puttner, I. B., and H. R. Kaback. 1988. lac permease of Escherichia coli containing a single histidine residue is fully functional. Proc. Natl. Acad. Sci. USA. 85:1467-1471.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1467-1471
    • Puttner, I.B.1    Kaback, H.R.2
  • 77
    • 0024562578 scopus 로고
    • Characterization of site-directed mutants in the lac permease of Escherichia coli. 2. Glutamate-325 replacements
    • Carrasco, N., I. B. Puttner, L. M. Antes, J. A. Lee, J. D. Larigan, J. S. Lolkema, P. D. Roepe, and H. R. Kaback. 1989. Characterization of site-directed mutants in the lac permease of Escherichia coli. 2. Glutamate-325 replacements. Biochemistry. 28:2533-2539.
    • (1989) Biochemistry , vol.28 , pp. 2533-2539
    • Carrasco, N.1    Puttner, I.B.2    Antes, L.M.3    Lee, J.A.4    Larigan, J.D.5    Lolkema, J.S.6    Roepe, P.D.7    Kaback, H.R.8
  • 78
    • 0039423890 scopus 로고    scopus 로고
    • Functional conservation in the putative substrate binding site of the sucrose permease from Escherichia coli
    • Sahin-Toth, M., and H. R. Kaback. 2000. Functional conservation in the putative substrate binding site of the sucrose permease from Escherichia coli. Biochemistry. 39:6170-6175.
    • (2000) Biochemistry , vol.39 , pp. 6170-6175
    • Sahin-Toth, M.1    Kaback, H.R.2
  • 79
    • 0035365996 scopus 로고    scopus 로고
    • A triple mutant, K319N/H322Q/E325Q, of the lactose permease cotransports H+ with thiodigalactoside
    • Johnson, J. L., M. S. Lockheart, and R. J. Brooker. 2001. A triple mutant, K319N/H322Q/E325Q, of the lactose permease cotransports H+ with thiodigalactoside. J. Membr. Biol. 181:215-224.
    • (2001) J. Membr. Biol , vol.181 , pp. 215-224
    • Johnson, J.L.1    Lockheart, M.S.2    Brooker, R.J.3
  • 80
    • 33645296826 scopus 로고    scopus 로고
    • ClC chloride channels viewed through a transporter lens 1
    • Miller, C. 2006. ClC chloride channels viewed through a transporter lens 1. Nature. 440:484-489.
    • (2006) Nature , vol.440 , pp. 484-489
    • Miller, C.1
  • 81
    • 0041836334 scopus 로고    scopus 로고
    • Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli
    • Ermolova, N., L. Guan, and H. R. Kaback. 2003. Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. USA. 100:10187-10192.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10187-10192
    • Ermolova, N.1    Guan, L.2    Kaback, H.R.3
  • 82
    • 0034609514 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix X
    • Venkatesan, P., Y. Hu, and H. R. Kaback. 2000. Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix X. Biochemistry. 39:10656-10661.
    • (2000) Biochemistry , vol.39 , pp. 10656-10661
    • Venkatesan, P.1    Hu, Y.2    Kaback, H.R.3
  • 83
    • 0034609552 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: N-ethylmaleimide-sensitive face of helix II
    • Venkatesan, P., Z. Liu, Y. Hu, and H. R. Kaback. 2000. Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: N-ethylmaleimide-sensitive face of helix II. Biochemistry. 39:10649-10655.
    • (2000) Biochemistry , vol.39 , pp. 10649-10655
    • Venkatesan, P.1    Liu, Z.2    Hu, Y.3    Kaback, H.R.4
  • 85
    • 0019330788 scopus 로고
    • Quantitative measurements of membrane potential in Escherichia coli
    • Felle, H., J. S. Porter, C. L. Slayman, and H. R. Kaback. 1980. Quantitative measurements of membrane potential in Escherichia coli. Biochemistry. 19:3585-3590.
    • (1980) Biochemistry , vol.19 , pp. 3585-3590
    • Felle, H.1    Porter, J.S.2    Slayman, C.L.3    Kaback, H.R.4
  • 86
    • 0346057931 scopus 로고    scopus 로고
    • Competition with xenon elicits ligand migration and escape pathways in myoglobin
    • Tetreau, C., Y. Blouquit, E. Novikov, E. Quiniou, and D. Lavalette. 2004. Competition with xenon elicits ligand migration and escape pathways in myoglobin. Biophys. J. 86:435-447.
    • (2004) Biophys. J , vol.86 , pp. 435-447
    • Tetreau, C.1    Blouquit, Y.2    Novikov, E.3    Quiniou, E.4    Lavalette, D.5
  • 87
    • 11744379062 scopus 로고
    • Fluctuation driven ratchets: Molecular motors
    • Astumian, R. D., and M. Bier. 1994. Fluctuation driven ratchets: molecular motors. Phys. Rev. Lett. 72:1766-1769.
    • (1994) Phys. Rev. Lett , vol.72 , pp. 1766-1769
    • Astumian, R.D.1    Bier, M.2
  • 88
    • 0031003997 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of a Brownian motor
    • Astumian, R. D. 1997. Thermodynamics and kinetics of a Brownian motor. Science. 276:917-922.
    • (1997) Science , vol.276 , pp. 917-922
    • Astumian, R.D.1
  • 90
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxen, K., G. Gilderson, P. Adelroth, and P. Brzezinski. 2005. A mechanistic principle for proton pumping by cytochrome c oxidase. Nature. 437:286-289.
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxen, K.1    Gilderson, G.2    Adelroth, P.3    Brzezinski, P.4
  • 91
  • 93
    • 0345698978 scopus 로고    scopus 로고
    • Fluctuation driven transport and models of molecular motors and pumps
    • Astumian, R. D., and I. Derenyi. 1998. Fluctuation driven transport and models of molecular motors and pumps. Eur. Biophys. J. 27:474-489.
    • (1998) Eur. Biophys. J , vol.27 , pp. 474-489
    • Astumian, R.D.1    Derenyi, I.2
  • 94
    • 0023512783 scopus 로고
    • Electroconformational coupling and membrane protein function
    • Tsong, T. Y., and R. D. Astumian. 1987. Electroconformational coupling and membrane protein function. Prog. Biophys. Mol. Biol. 50:1-45.
    • (1987) Prog. Biophys. Mol. Biol , vol.50 , pp. 1-45
    • Tsong, T.Y.1    Astumian, R.D.2
  • 95
    • 0036928486 scopus 로고    scopus 로고
    • Flux coupling in the human serotonin transporter
    • Adams, S. V., and L. J. DeFelice. 2002. Flux coupling in the human serotonin transporter. Biophys. J. 83:3268-3282.
    • (2002) Biophys. J , vol.83 , pp. 3268-3282
    • Adams, S.V.1    DeFelice, L.J.2
  • 96
    • 0034815183 scopus 로고    scopus 로고
    • Single-file diffusion and neurotransmitter transporters: Hodgkin and Keynes model revisited
    • DeFelice, L. J., S. V. Adams, and D. L. Ypey. 2001. Single-file diffusion and neurotransmitter transporters: Hodgkin and Keynes model revisited. Biosystems. 62:57-66.
    • (2001) Biosystems , vol.62 , pp. 57-66
    • DeFelice, L.J.1    Adams, S.V.2    Ypey, D.L.3
  • 98
    • 11744376328 scopus 로고
    • An unexpected symmetry of the Coulomb potential in the Debye-Smoluchowski equation
    • Clifford, P., N. J. B. Green, and M. J. Pilling. 1982. An unexpected symmetry of the Coulomb potential in the Debye-Smoluchowski equation. Chem. Phys. Lett. 91:101-108.
    • (1982) Chem. Phys. Lett , vol.91 , pp. 101-108
    • Clifford, P.1    Green, N.J.B.2    Pilling, M.J.3
  • 100
    • 84976811726 scopus 로고
    • Algorithm 471-exponential integrals
    • Gautschi, W. 1973. Algorithm 471-exponential integrals. Commun. ACM. 16:761-763.
    • (1973) Commun. ACM , vol.16 , pp. 761-763
    • Gautschi, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.