메뉴 건너뛰기




Volumn 328, Issue 6 SPEC. ISS., 2005, Pages 557-567

Structure and mechanism of the lactose permease

Author keywords

Bioenergetics; lac Operon; Membrane proteins; Transport

Indexed keywords

LACTOSE PERMEASE; MEMBRANE PROTEIN;

EID: 20444419395     PISSN: 16310691     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.crvi.2005.03.008     Document Type: Short Survey
Times cited : (81)

References (73)
  • 1
    • 0000413253 scopus 로고
    • Molecule, group and electron transport through natural membranes
    • P. Mitchell Molecule, group and electron transport through natural membranes Biochem. Soc. Symp. 22 1963 142-168
    • (1963) Biochem. Soc. Symp. , vol.22 , pp. 142-168
    • Mitchell, P.1
  • 3
    • 0017049441 scopus 로고
    • Molecular biology and energetics of membrane transport
    • H.R. Kaback Molecular biology and energetics of membrane transport J. Cell Physiol. 89 1976 575-593
    • (1976) J. Cell Physiol. , vol.89 , pp. 575-593
    • Kaback, H.R.1
  • 4
    • 0021066915 scopus 로고
    • The lac carrier protein in Escherichia coli: From membrane to molecule
    • H.R. Kaback The lac carrier protein in Escherichia coli: From membrane to molecule J. Membr. Biol. 76 1983 95-112
    • (1983) J. Membr. Biol. , vol.76 , pp. 95-112
    • Kaback, H.R.1
  • 5
    • 0023530232 scopus 로고
    • Molecular biology of active transport: From membranes to molecules to mechanism
    • H.R. Kaback Molecular biology of active transport: From membranes to molecules to mechanism Harvey Lect. 83 1989 77-103
    • (1989) Harvey Lect. , vol.83 , pp. 77-103
    • Kaback, H.R.1
  • 7
    • 0017839043 scopus 로고
    • Amplification of the lactose carrier protein in Escherichia coli using a plasmid vector
    • R.M. Teather B. Müller-Hill U. Abrutsch G. Aichele P. Overath Amplification of the lactose carrier protein in Escherichia coli using a plasmid vector Mol. Gen. Genet. 159 1978 239-248
    • (1978) Mol. Gen. Genet. , vol.159 , pp. 239-248
    • Teather, R.M.1    Müller-Hill, B.2    Abrutsch, U.3    Aichele, G.4    Overath, P.5
  • 9
    • 0019888608 scopus 로고
    • Purification and reconstitution of functional lactose carrier from Escherichia coli
    • M.J. Newman D.L. Foster T.H. Wilson H.R. Kaback Purification and reconstitution of functional lactose carrier from Escherichia coli J. Biol. Chem. 256 1981 11804-11808
    • (1981) J. Biol. Chem. , vol.256 , pp. 11804-11808
    • Newman, M.J.1    Foster, D.L.2    Wilson, T.H.3    Kaback, H.R.4
  • 10
    • 0021269079 scopus 로고
    • Purified reconstituted lac carrier protein from Escherichia coli is fully functional
    • P. Viitanen M.L. Garcia H.R. Kaback Purified reconstituted lac carrier protein from Escherichia coli is fully functional Proc. Natl Acad. Sci. USA 81 1984 1629-1633
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1629-1633
    • Viitanen, P.1    Garcia, M.L.2    Kaback, H.R.3
  • 11
    • 0028291250 scopus 로고
    • Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli
    • M. Sahin-Tóth M.C. Lawrence H.R. Kaback Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli Proc. Natl Acad. Sci. USA 91 1994 5421-5425
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5421-5425
    • Sahin-Tóth, M.1    Lawrence, M.C.2    Kaback, H.R.3
  • 12
    • 0037133698 scopus 로고    scopus 로고
    • Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking
    • L. Guan F.D. Murphy H.R. Kaback Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking Proc. Natl Acad. Sci. USA 99 2002 3475-3480
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3475-3480
    • Guan, L.1    Murphy, F.D.2    Kaback, H.R.3
  • 13
    • 0041836334 scopus 로고    scopus 로고
    • Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli
    • N. Ermolova L. Guan H.R. Kaback Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli Proc. Natl Acad. Sci. USA 100 2003 10187-10192
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10187-10192
    • Ermolova, N.1    Guan, L.2    Kaback, H.R.3
  • 15
    • 0033977101 scopus 로고    scopus 로고
    • Families of transmembrane sugar transport proteins
    • M.H. Saier Jr. Families of transmembrane sugar transport proteins Mol. Microbiol. 35 2000 699-710
    • (2000) Mol. Microbiol. , vol.35 , pp. 699-710
    • Saier Jr., M.H.1
  • 16
    • 0020681373 scopus 로고
    • Structure of the lac carrier protein of Escherichia coli
    • D.L. Foster M. Boublik H.R. Kaback Structure of the lac carrier protein of Escherichia coli J. Biol. Chem. 258 1983 31-34
    • (1983) J. Biol. Chem. , vol.258 , pp. 31-34
    • Foster, D.L.1    Boublik, M.2    Kaback, H.R.3
  • 17
    • 0022427814 scopus 로고
    • The structure of the lactose permease derived from Raman spectroscopy and prediction methods
    • H. Vogel J.K. Wright F. Jähnig The structure of the lactose permease derived from Raman spectroscopy and prediction methods EMBO J. 4 1985 3625-3631
    • (1985) EMBO J. , vol.4 , pp. 3625-3631
    • Vogel, H.1    Wright, J.K.2    Jähnig, F.3
  • 18
    • 0030885252 scopus 로고    scopus 로고
    • The lipid bilayer determines helical tilt angle and function in lactose permease of Escherichia coli
    • J. Le Coutre L.R. Narasimhan C.K. Patel H.R. Kaback The lipid bilayer determines helical tilt angle and function in lactose permease of Escherichia coli Proc. Natl Acad. Sci. USA 94 1997 10167-10171
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10167-10171
    • Le Coutre, J.1    Narasimhan, L.R.2    Patel, C.K.3    Kaback, H.R.4
  • 19
    • 0032480817 scopus 로고    scopus 로고
    • Fourier transform infrared analysis of purified lactose permease: A monodisperse lactose permease preparation is stably folded, alpha-helical, and highly accessible to deuterium exchange
    • J.S. Patzlaff J.A. Moeller B.A. Barry R.J. Brooker Fourier transform infrared analysis of purified lactose permease: A monodisperse lactose permease preparation is stably folded, alpha-helical, and highly accessible to deuterium exchange Biochemistry 37 1998 15363-15375
    • (1998) Biochemistry , vol.37 , pp. 15363-15375
    • Patzlaff, J.S.1    Moeller, J.A.2    Barry, B.A.3    Brooker, R.J.4
  • 20
    • 0025330038 scopus 로고
    • Lac permease of Escherichia coli: Topology and sequence elements promoting membrane insertion
    • J. Calamia C. Manoil Lac permease of Escherichia coli: Topology and sequence elements promoting membrane insertion Proc. Natl Acad. Sci. USA 87 1990 4937-4941
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4937-4941
    • Calamia, J.1    Manoil, C.2
  • 21
    • 0033614794 scopus 로고    scopus 로고
    • Estimating loop-helix interfaces in a polytopic membrane protein by deletion analysis
    • C. Wolin H.R. Kaback Estimating loop-helix interfaces in a polytopic membrane protein by deletion analysis Biochemistry 38 1999 8590-8597
    • (1999) Biochemistry , vol.38 , pp. 8590-8597
    • Wolin, C.1    Kaback, H.R.2
  • 22
    • 0035916241 scopus 로고    scopus 로고
    • Functional estimation of loop-helix boundaries in the lactose permease of Escherichia coli by single amino acid deletion analysis
    • C.D. Wolin H.R. Kaback Functional estimation of loop-helix boundaries in the lactose permease of Escherichia coli by single amino acid deletion analysis Biochemistry 40 2001 1996-2003
    • (2001) Biochemistry , vol.40 , pp. 1996-2003
    • Wolin, C.D.1    Kaback, H.R.2
  • 23
    • 0031776931 scopus 로고    scopus 로고
    • Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins
    • J.P. Whitelegge C.B. Gundersen K.F. Faull Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins Protein Sci. 7 1998 1423-1430
    • (1998) Protein Sci. , vol.7 , pp. 1423-1430
    • Whitelegge, J.P.1    Gundersen, C.B.2    Faull, K.F.3
  • 26
    • 0034467682 scopus 로고    scopus 로고
    • Structure-function relationships of integral membrane proteins: Membrane transporters vs channels
    • J. Le Coutre H.R. Kaback Structure-function relationships of integral membrane proteins: Membrane transporters vs channels Biopolymers 55 2000 297-307
    • (2000) Biopolymers , vol.55 , pp. 297-307
    • Le Coutre, J.1    Kaback, H.R.2
  • 27
    • 0344838440 scopus 로고    scopus 로고
    • Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry
    • A.B. Weinglass J.P. Whitelegge Y. Hu G.E. Verner K.F. Faull H.R. Kaback Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry EMBO J. 22 2003 1467-1477
    • (2003) EMBO J. , vol.22 , pp. 1467-1477
    • Weinglass, A.B.1    Whitelegge, J.P.2    Hu, Y.3    Verner, G.E.4    Faull, K.F.5    Kaback, H.R.6
  • 28
    • 0018837284 scopus 로고
    • In vitro and in vivo products of E. coli lactose permease gene are identical
    • R. Ehring K. Beyreuther J.K. Wright P. Overath In vitro and in vivo products of E. coli lactose permease gene are identical Nature 283 1980 537-540
    • (1980) Nature , vol.283 , pp. 537-540
    • Ehring, R.1    Beyreuther, K.2    Wright, J.K.3    Overath, P.4
  • 30
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure function relationships in polytopic membrane proteins
    • S. Frillingos M. Sahin-Toth J. Wu H.R. Kaback Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins FASEB J. 12 1998 1281-1299
    • (1998) FASEB J. , vol.12 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Toth, M.2    Wu, J.3    Kaback, H.R.4
  • 31
    • 0031398840 scopus 로고    scopus 로고
    • From membrane to molecule to the third amino acid from the left with the lactose permease of Escherichia coli
    • H.R. Kaback J. Wu From membrane to molecule to the third amino acid from the left with the lactose permease of Escherichia coli Quart. Rev. Biophys. 30 1997 333-364
    • (1997) Quart. Rev. Biophys. , vol.30 , pp. 333-364
    • Kaback, H.R.1    Wu, J.2
  • 33
    • 77049146099 scopus 로고
    • Inability of diffusion to account for placental glucose transfer in the sheep and consideration of the kinetics of a possible carrier transfer
    • W.F. Widdas Inability of diffusion to account for placental glucose transfer in the sheep and consideration of the kinetics of a possible carrier transfer J. Physiol. 118 1952 23-39
    • (1952) J. Physiol. , vol.118 , pp. 23-39
    • Widdas, W.F.1
  • 34
    • 0037373068 scopus 로고    scopus 로고
    • Structural model for 12-helix transporters belonging to the major facilitator superfamily
    • T. Hirai J.A. Heymann P.C. Maloney S. Subramaniam Structural model for 12-helix transporters belonging to the major facilitator superfamily J. Bacteriol. 185 2003 1712-1718
    • (2003) J. Bacteriol. , vol.185 , pp. 1712-1718
    • Hirai, T.1    Heymann, J.A.2    Maloney, P.C.3    Subramaniam, S.4
  • 35
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Y. Huang M.-J. Lemieux J. Song M. Auer D.N. Wang Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli Science 301 2003 616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.-J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 36
    • 0030685033 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential
    • S. Frillingos A. Gonzalez H.R. Kaback Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential Biochemistry 36 1997 14284-14290
    • (1997) Biochemistry , vol.36 , pp. 14284-14290
    • Frillingos, S.1    Gonzalez, A.2    Kaback, H.R.3
  • 37
    • 0034609514 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix X
    • P. Venkatesan Y. Hu H.R. Kaback Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix X Biochemistry 39 2000 10656-10661
    • (2000) Biochemistry , vol.39 , pp. 10656-10661
    • Venkatesan, P.1    Hu, Y.2    Kaback, H.R.3
  • 38
    • 0038257492 scopus 로고    scopus 로고
    • Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli
    • M. Sahin-Tóth J. Le Coutre D. Kharabi G. Le Maire J.C. Lee H.R. Kaback Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli Biochemistry 38 1999 813-819
    • (1999) Biochemistry , vol.38 , pp. 813-819
    • Sahin-Tóth, M.1    Le Coutre, J.2    Kharabi, D.3    Le Maire, G.4    Lee, J.C.5    Kaback, H.R.6
  • 39
    • 0034718616 scopus 로고    scopus 로고
    • Unraveling the mechanism of lactose permease of Escherichia coli
    • M. Sahin-Tóth A. Karlin H.R. Kaback Unraveling the mechanism of lactose permease of Escherichia coli Proc. Natl Acad. Sci. USA 97 2000 10729-10732
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10729-10732
    • Sahin-Tóth, M.1    Karlin, A.2    Kaback, H.R.3
  • 40
    • 0034705079 scopus 로고    scopus 로고
    • Thiol cross-linking of transmembrane domains IV and V in the lactose permease of Escherichia coli
    • C.D. Wolin H.R. Kaback Thiol cross-linking of transmembrane domains IV and V in the lactose permease of Escherichia coli Biochemistry 39 2000 6130-6135
    • (2000) Biochemistry , vol.39 , pp. 6130-6135
    • Wolin, C.D.1    Kaback, H.R.2
  • 41
    • 0033535984 scopus 로고    scopus 로고
    • Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli
    • M. Zhao K.C. Zen W.L. Hubbell H.R. Kaback Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli Biochemistry 38 1999 7407-7412
    • (1999) Biochemistry , vol.38 , pp. 7407-7412
    • Zhao, M.1    Zen, K.C.2    Hubbell, W.L.3    Kaback, H.R.4
  • 42
    • 4744348289 scopus 로고    scopus 로고
    • Monitoring conformational rearrangements in the substrate-binding site of a membrane transport protein by mass spectrometry
    • A. Weinglass J.P. Whitelegge K.F. Faull H.R. Kaback Monitoring conformational rearrangements in the substrate-binding site of a membrane transport protein by mass spectrometry J. Biol. Chem. 279 2004 41858-41865
    • (2004) J. Biol. Chem. , vol.279 , pp. 41858-41865
    • Weinglass, A.1    Whitelegge, J.P.2    Faull, K.F.3    Kaback, H.R.4
  • 43
    • 0037452555 scopus 로고    scopus 로고
    • Aromatic stacking in the sugar binding site of the lactose permease
    • L. Guan Y. Hu H.R. Kaback Aromatic stacking in the sugar binding site of the lactose permease Biochemistry 42 2003 1377-1382
    • (2003) Biochemistry , vol.42 , pp. 1377-1382
    • Guan, L.1    Hu, Y.2    Kaback, H.R.3
  • 44
    • 0242363172 scopus 로고    scopus 로고
    • Exploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli
    • J.L. Vazquez-Ibar L. Guan M. Svrakic H.R. Kaback Exploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli Proc. Natl Acad. Sci. USA 100 2003 12706-12711
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12706-12711
    • Vazquez-Ibar, J.L.1    Guan, L.2    Svrakic, M.3    Kaback, H.R.4
  • 45
    • 0031573456 scopus 로고    scopus 로고
    • Structural foundation for the design of receptor antagonists targeting Escherichia coli heat-labile enterotoxin
    • E.A. Merritt S. Sarfaty I.K. Feil W.G. Hol Structural foundation for the design of receptor antagonists targeting Escherichia coli heat-labile enterotoxin Structure 5 1997 1485-1499
    • (1997) Structure , vol.5 , pp. 1485-1499
    • Merritt, E.A.1    Sarfaty, S.2    Feil, I.K.3    Hol, W.G.4
  • 50
    • 0028234751 scopus 로고
    • Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli
    • P.J. Franco R.J. Brooker Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli J. Biol. Chem. 269 1994 7379-7386
    • (1994) J. Biol. Chem. , vol.269 , pp. 7379-7386
    • Franco, P.J.1    Brooker, R.J.2
  • 51
    • 0036300742 scopus 로고    scopus 로고
    • Manipulating conformational equilibria in the lactose permease of Escherichia coli
    • A.B. Weinglass M. Sondej H.R. Kaback Manipulating conformational equilibria in the lactose permease of Escherichia coli J. Mol. Biol. 315 2002 561-571
    • (2002) J. Mol. Biol. , vol.315 , pp. 561-571
    • Weinglass, A.B.1    Sondej, M.2    Kaback, H.R.3
  • 52
    • 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
    • M. Sahin-Tóth K.M. Akhoon J. Runner H.R. Kaback Ligand recognition by the lactose permease of Escherichia coli: Specificity and affinity are defined by distinct structural elements of galactopyranosides Biochemistry 39 2000 5097-5103
    • (2000) Biochemistry , vol.39 , pp. 5097-5103
    • Sahin-Tóth, M.1    Akhoon, K.M.2    Runner, J.3    Kaback, H.R.4
  • 53
    • 0026439214 scopus 로고
    • Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli
    • M. Sahin-Tóth R.L. Dunten A. Gonzalez H.R. Kaback Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli Proc. Natl Acad. Sci. USA 89 1992 10547-10551
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10547-10551
    • Sahin-Tóth, M.1    Dunten, R.L.2    Gonzalez, A.3    Kaback, H.R.4
  • 54
    • 0027382884 scopus 로고
    • Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli
    • M. Sahin-Tóth H.R. Kaback Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli Biochemistry 32 1993 10027-10035
    • (1993) Biochemistry , vol.32 , pp. 10027-10035
    • Sahin-Tóth, M.1    Kaback, H.R.2
  • 55
    • 0027419744 scopus 로고
    • Role of the charge pair formed by aspartic acid 237 and lysine 358 in the lactose permease of Escherichia coli
    • R.L. Dunten M. Sahin-Tóth H.R. Kaback Role of the charge pair formed by aspartic acid 237 and lysine 358 in the lactose permease of Escherichia coli Biochemistry 32 1993 3139-3145
    • (1993) Biochemistry , vol.32 , pp. 3139-3145
    • Dunten, R.L.1    Sahin-Tóth, M.2    Kaback, H.R.3
  • 56
    • 0035980232 scopus 로고    scopus 로고
    • The C-4 hydroxyl group of galactopyranosides is the major determinant for ligand recognition by the lactose permease of Escherichia coli
    • M. Sahin-Tóth M.C. Lawrence T. Nishio H.R. Kaback The C-4 hydroxyl group of galactopyranosides is the major determinant for ligand recognition by the lactose permease of Escherichia coli Biochemistry 43 2001 13015-13019
    • (2001) Biochemistry , vol.43 , pp. 13015-13019
    • Sahin-Tóth, M.1    Lawrence, M.C.2    Nishio, T.3    Kaback, H.R.4
  • 57
    • 1642297145 scopus 로고    scopus 로고
    • Direct evidence for substrate-induced proton release in detergent-solubilized EmrE, a multidrug transporter
    • M. Soskine Y. Adam S. Schuldiner Direct evidence for substrate-induced proton release in detergent-solubilized EmrE, a multidrug transporter J. Biol. Chem. 279 2004 9951-9955
    • (2004) J. Biol. Chem. , vol.279 , pp. 9951-9955
    • Soskine, M.1    Adam, Y.2    Schuldiner, S.3
  • 59
    • 0035932954 scopus 로고    scopus 로고
    • Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichia coli
    • M. Sahin-Tóth H.R. Kaback Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichia coli Proc. Natl Acad. Sci. USA 98 2001 6068-6073
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6068-6073
    • Sahin-Tóth, M.1    Kaback, H.R.2
  • 60
    • 0027375714 scopus 로고
    • Use of site-directed fluorescence labeling to study proximity relationships in the lactose permease of Escherichia coli
    • K. Jung H. Jung J. Wu G.G. Privé H.R. Kaback Use of site-directed fluorescence labeling to study proximity relationships in the lactose permease of Escherichia coli Biochemistry 32 1993 12273-12278
    • (1993) Biochemistry , vol.32 , pp. 12273-12278
    • Jung, K.1    Jung, H.2    Wu, J.3    Privé, G.G.4    Kaback, H.R.5
  • 61
    • 0029041299 scopus 로고
    • Engineering a metal binding site within a polytopic membrane protein, the lactose permease of Escherichia coli
    • K. Jung J. Voss M. He W.L. Hubbell H.R. Kaback Engineering a metal binding site within a polytopic membrane protein, the lactose permease of Escherichia coli Biochemistry 34 1995 6272-6277
    • (1995) Biochemistry , vol.34 , pp. 6272-6277
    • Jung, K.1    Voss, J.2    He, M.3    Hubbell, W.L.4    Kaback, H.R.5
  • 62
    • 0030771680 scopus 로고    scopus 로고
    • Interaction between residues Glu269 (Helix VIII) and His322 (Helix X) of the lactose permease of Escherichia coli is essential for substrate binding
    • M. He H.R. Kaback Interaction between residues Glu269 (Helix VIII) and His322 (Helix X) of the lactose permease of Escherichia coli is essential for substrate binding Biochemistry 36 1997 13688-13692
    • (1997) Biochemistry , vol.36 , pp. 13688-13692
    • He, M.1    Kaback, H.R.2
  • 63
    • 0019297953 scopus 로고
    • Active transport in membrane vesicles from Escherichia coli: The electrochemical proton gradient alters the distribution of the lac carrier between two different kinetic states
    • D.E. Robertson G.J. Kaczorowski M.L. Garcia H.R. Kaback Active transport in membrane vesicles from Escherichia coli: The electrochemical proton gradient alters the distribution of the lac carrier between two different kinetic states Biochemistry 19 1980 5692-5702
    • (1980) Biochemistry , vol.19 , pp. 5692-5702
    • Robertson, D.E.1    Kaczorowski, G.J.2    Garcia, M.L.3    Kaback, H.R.4
  • 64
    • 0017063727 scopus 로고
    • The electrochemical gradient of protons and its relationship to active transport in Escherichia coli membrane vesicles
    • S. Ramos S. Schuldiner H.R. Kaback The electrochemical gradient of protons and its relationship to active transport in Escherichia coli membrane vesicles Proc. Natl Acad. Sci. USA 73 1976 1892-1896
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1892-1896
    • Ramos, S.1    Schuldiner, S.2    Kaback, H.R.3
  • 65
    • 0017616591 scopus 로고
    • The relationship between the electrochemical proton gradient and active transport in Escherichia coli membrane vesicles
    • S. Ramos H.R. Kaback The relationship between the electrochemical proton gradient and active transport in Escherichia coli membrane vesicles Biochemistry 16 1977 854-859
    • (1977) Biochemistry , vol.16 , pp. 854-859
    • Ramos, S.1    Kaback, H.R.2
  • 66
    • 0029931067 scopus 로고    scopus 로고
    • Probing the conformation of the lactose permease of Escherichia coli by in situ site-directed sulfhydryl modification
    • S. Frillingos H.R. Kaback Probing the conformation of the lactose permease of Escherichia coli by in situ site-directed sulfhydryl modification Biochemistry 35 1996 3950-3956
    • (1996) Biochemistry , vol.35 , pp. 3950-3956
    • Frillingos, S.1    Kaback, H.R.2
  • 67
    • 0032544066 scopus 로고    scopus 로고
    • The substrate binding site in the lactose permease of Escherichia coli
    • P. Venkatesan H.R. Kaback The substrate binding site in the lactose permease of Escherichia coli Proc. Natl Acad. Sci. USA 95 1998 9802-9807
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9802-9807
    • Venkatesan, P.1    Kaback, H.R.2
  • 68
    • 0037195244 scopus 로고    scopus 로고
    • Binding of hydrophobic d-galactopyranosides to the lactose permease of Escherichia coli
    • M. Sahin-Tóth P. Gunawan M.C. Lawrence T. Toyokuni H.R. Kaback Binding of hydrophobic d-galactopyranosides to the lactose permease of Escherichia coli Biochemistry 41 2002 13039-13045
    • (2002) Biochemistry , vol.41 , pp. 13039-13045
    • Sahin-Tóth, M.1    Gunawan, P.2    Lawrence, M.C.3    Toyokuni, T.4    Kaback, H.R.5
  • 70
    • 0015218481 scopus 로고
    • Mechanisms of active transport in isolated membrane vesicles. II. The mechanism of energy coupling between d-lactic dehydrogenase and β-galactoside transport in membrane preparations from Escherichia coli
    • H.R. Kaback E.M. Barnes Jr. Mechanisms of active transport in isolated membrane vesicles. II. The mechanism of energy coupling between d-lactic dehydrogenase and β-galactoside transport in membrane preparations from Escherichia coli J. Biol. Chem. 246 1971 5523-5531
    • (1971) J. Biol. Chem. , vol.246 , pp. 5523-5531
    • Kaback, H.R.1    Barnes Jr., E.M.2
  • 71
    • 0018841199 scopus 로고
    • Electrochemical proton gradient in inverted membrane vesicles from Escherichia coli
    • W.W. Reenstra L. Patel H. Rottenberg H.R. Kaback Electrochemical proton gradient in inverted membrane vesicles from Escherichia coli Biochemistry 19 1980 1-9
    • (1980) Biochemistry , vol.19 , pp. 1-9
    • Reenstra, W.W.1    Patel, L.2    Rottenberg, H.3    Kaback, H.R.4
  • 73
    • 0020536680 scopus 로고
    • Mechanism of lactose translocation in proteoliposomes reconstituted with lac carrier protein purified from Escherichia coli. 2. Deuterium solvent isotope effects
    • P. Viitanen M.L. Garcia D.L. Foster G.J. Kaczorowski H.R. Kaback Mechanism of lactose translocation in proteoliposomes reconstituted with lac carrier protein purified from Escherichia coli. 2. Deuterium solvent isotope effects Biochemistry 22 1983 2531-2536
    • (1983) Biochemistry , vol.22 , pp. 2531-2536
    • Viitanen, P.1    Garcia, M.L.2    Foster, D.L.3    Kaczorowski, G.J.4    Kaback, H.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.