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Volumn 109, Issue 31, 2012, Pages 12438-12442

Role of the irreplaceable residues in the LacY alternating access mechanism

Author keywords

Membrane protein; Membranes; Protein dynamics; Transport

Indexed keywords

GALACTOSIDE; LACTOSE PERMEASE; SUGAR;

EID: 84864526188     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1210684109     Document Type: Article
Times cited : (14)

References (52)
  • 2
    • 0022558555 scopus 로고
    • Purification, reconstitution, and characterization of the lac permease of Escherichia coli
    • Viitanen P, Newman MJ, Foster DL, Wilson TH, Kaback HR (1986) Purification, reconstitution, and characterization of the lac permease of Escherichia coli. Methods Enzymol 125:429-452. (Pubitemid 16072654)
    • (1986) Methods in Enzymology , vol.VOL. 125 , pp. 429-452
    • Viitanen, P.1    Newman, M.J.2    Foster, D.L.3
  • 3
    • 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
    • DOI 10.1073/pnas.052703699
    • Guan L, Murphy FD, Kaback HR (2002) 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 99:3475-3480. (Pubitemid 34252133)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.6 , pp. 3475-3480
    • Guan, L.1    Murphy, F.D.2    Kaback, H.R.3
  • 6
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • DOI 10.1126/science.1088196
    • Abramson J, et al. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301:610-615. (Pubitemid 36927939)
    • (2003) Science , vol.301 , Issue.5633 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 7
    • 33645320817 scopus 로고    scopus 로고
    • Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY
    • Mirza O, Guan L, Verner G, Iwata S, Kaback HR (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
  • 9
    • 79959349280 scopus 로고    scopus 로고
    • Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
    • Chaptal V, et al. (2011) Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition. Proc Natl Acad Sci USA 108:9361-9366.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 9361-9366
    • Chaptal, V.1
  • 13
    • 35548929298 scopus 로고    scopus 로고
    • Site-directed Alkylation of LacY: Effect of the Proton Electrochemical Gradient
    • DOI 10.1016/j.jmb.2007.09.006, PII S0022283607011679
    • Nie Y, Ermolova N, Kaback HR (2007) Site-directed alkylation of LacY: Effect of the proton electrochemical gradient. J Mol Biol 374:356-364. (Pubitemid 350007643)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.2 , pp. 356-364
    • Nie, Y.1    Ermolova, N.2    Kaback, H.R.3
  • 14
    • 44149122380 scopus 로고    scopus 로고
    • The Cys154 - >Gly mutation in LacY causes constitutive opening of the hydrophilic periplasmic pathway
    • Nie Y, Sabetfard FE, Kaback HR (2008) The Cys154 - >Gly mutation in LacY causes constitutive opening of the hydrophilic periplasmic pathway. J Mol Biol 379:695-703.
    • (2008) J Mol Biol , vol.379 , pp. 695-703
    • Nie, Y.1    Sabetfard, F.E.2    Kaback, H.R.3
  • 16
    • 77953101915 scopus 로고    scopus 로고
    • Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane
    • Nie Y, Kaback HR (2010) Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane. Proc Natl Acad Sci USA 107:9903-9908.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9903-9908
    • Nie, Y.1    Kaback, H.R.2
  • 17
    • 79952369030 scopus 로고    scopus 로고
    • Site-directed alkylation studies with LacY provide evidence for the alternating access model of transport
    • Jiang X, Nie Y, Kaback HR (2011) Site-directed alkylation studies with LacY provide evidence for the alternating access model of transport. Biochemistry 50:1634-1640.
    • (2011) Biochemistry , vol.50 , pp. 1634-1640
    • Jiang, X.1    Nie, Y.2    Kaback, H.R.3
  • 19
    • 80053056248 scopus 로고    scopus 로고
    • Opening the periplasmic cavity in lactose permease is the limiting step for sugar binding
    • Smirnova I, Kasho V, Sugihara J, Kaback HR (2011) Opening the periplasmic cavity in lactose permease is the limiting step for sugar binding. Proc Natl Acad Sci USA 108:15147-15151.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 15147-15151
    • Smirnova, I.1    Kasho, V.2    Sugihara, J.3    Kaback, H.R.4
  • 20
    • 53849119555 scopus 로고    scopus 로고
    • Ins and outs of major facilitator superfamily antiporters
    • Law CJ, Maloney PC, Wang DN (2008) Ins and outs of major facilitator superfamily antiporters. Annu Rev Microbiol 62:289-305.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 289-305
    • Law, C.J.1    Maloney, P.C.2    Wang, D.N.3
  • 21
    • 84855351908 scopus 로고    scopus 로고
    • Insights into transport mechanism from LeuT engineered to transport tryptopan
    • Piscitelli CL, Gouaux B (2011) Insights into transport mechanism from LeuT engineered to transport tryptopan. EMBO J 31:228-235.
    • (2011) EMBO J , vol.31 , pp. 228-235
    • Piscitelli, C.L.1    Gouaux, B.2
  • 22
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outwardopen and apo inward-open states
    • Krishnamurthy H, Gouaux E (2012) X-ray structures of LeuT in substrate-free outwardopen and apo inward-open states. Nature 481:469-474.
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 23
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • DOI 10.1038/nature05155, PII NATURE05155
    • Dawson RJ, Locher KP (2006) Structure of a bacterial multidrug ABC transporter. Nature 443:180-185. (Pubitemid 44387602)
    • (2006) Nature , vol.443 , Issue.7108 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 24
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D, Oldham ML, Orelle C, Davidson AL, Chen J (2009) Alternating access in maltose transporter mediated by rigid-body rotations. Mol Cell 33:528-536.
    • (2009) Mol Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 25
    • 76049089794 scopus 로고    scopus 로고
    • Probing of the rates of alternating access in LacY with Trp fluorescence
    • Smirnova I, Kasho V, Sugihara J, Kaback HR (2009) Probing of the rates of alternating access in LacY with Trp fluorescence. Proc Natl Acad Sci USA 106:21561-21566.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21561-21566
    • Smirnova, I.1    Kasho, V.2    Sugihara, J.3    Kaback, H.R.4
  • 26
    • 84863369867 scopus 로고    scopus 로고
    • Evidence for an intermediate conformational state of LacY
    • Jiang X, et al. (2012) Evidence for an intermediate conformational state of LacY. Proc Natl Acad Sci USA 109:E698-E704.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Jiang, X.1
  • 27
    • 0030885252 scopus 로고    scopus 로고
    • The lipid bilayer determines helical tilt angle and function in lactose permease of Escherichia coli
    • le Coutre J, Narasimhan LR, Patel CK, Kaback HR (1997) The lipid bilayer determines helical tilt angle and function in lactose permease of Escherichia coli. Proc Natl Acad Sci USA 94:10167-10171.
    • (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
  • 28
    • 0032568559 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy reveals a rigid alpha-helical assembly for the tetrameric Streptomyces lividans K+ channel
    • le Coutre J, Kaback HR, Patel CK, Heginbotham L, Miller C (1998) Fourier transform infrared spectroscopy reveals a rigid alpha-helical assembly for the tetrameric Streptomyces lividans K+ channel. Proc Natl Acad Sci USA 95:6114-6117.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6114-6117
    • Le Coutre, J.1    Kaback, H.R.2    Patel, C.K.3    Heginbotham, L.4    Miller, C.5
  • 29
    • 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
    • DOI 10.1021/bi981142x
    • Patzlaff JS, Moeller JA, Barry BA, Brooker RJ (1998) 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 37:15363-15375. (Pubitemid 28515997)
    • (1998) Biochemistry , vol.37 , Issue.44 , pp. 15363-15375
    • Patzlaff, J.S.1    Moeller, J.A.2    Barry, B.A.3    Brooker, R.J.4
  • 30
    • 33845917073 scopus 로고    scopus 로고
    • Energetics of ligand-induced conformational flexibility in the lactose permease of Escherichia coli
    • DOI 10.1074/jbc.M607232200
    • Nie Y, Smirnova I, Kasho V, Kaback HR (2006) Energetics of ligand-induced conformational flexibility in the lactose permease of Escherichia coli. J Biol Chem 281:35779-35784. (Pubitemid 46041309)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 35779-35784
    • Nie, Y.1    Smirnova, I.2    Kasho, V.3    Kaback, H.R.4
  • 31
    • 65249190326 scopus 로고    scopus 로고
    • Structural characterization of the osmosensor ProP
    • Sayeed WM, Baenziger JE (2009) Structural characterization of the osmosensor ProP. Biochim Biophys Acta 1788:1108-1115.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1108-1115
    • Sayeed, W.M.1    Baenziger, J.E.2
  • 32
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure-function relationships in polytopic membrane proteins
    • Frillingos S, Sahin-Tóth M, Wu J, Kaback HR (1998) Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins. FASEB J 12:1281-1299. (Pubitemid 28475570)
    • (1998) FASEB Journal , vol.12 , Issue.13 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Toth, M.2    Wu, J.3    Kaback, H.R.4
  • 34
    • 80755122853 scopus 로고    scopus 로고
    • Lactose permease and the alternating access mechanism
    • Smirnova I, Kasho V, Kaback HR (2011) Lactose permease and the alternating access mechanism. Biochemistry 50:9684-9693.
    • (2011) Biochemistry , vol.50 , pp. 9684-9693
    • Smirnova, I.1    Kasho, V.2    Kaback, H.R.3
  • 35
    • 70349140554 scopus 로고    scopus 로고
    • Residues in the H+ translocation site define the pKa for sugar binding to LacY
    • Smirnova IN, Kasho VN, Sugihara J, Choe JY, Kaback HR (2009) Residues in the H+ translocation site define the pKa for sugar binding to LacY. Biochemistry 48:8852-8860.
    • (2009) Biochemistry , vol.48 , pp. 8852-8860
    • Smirnova, I.N.1    Kasho, V.N.2    Sugihara, J.3    Choe, J.Y.4    Kaback, H.R.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
    • DOI 10.1021/bi972314d
    • Frillingos S, Gonzalez A, Kaback HR (1997) Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential. off. Biochemistry 36:14284-14290. (Pubitemid 27509920)
    • (1997) Biochemistry , vol.36 , Issue.47 , pp. 14284-14290
    • Frillingos, S.1    Gonzalez, A.2    Kaback, H.R.3
  • 37
    • 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
    • Sahin-Tóth M, et al. (1999) Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli. Biochemistry 38:813-819.
    • (1999) Biochemistry , vol.38 , pp. 813-819
    • Sahin-Tóth, M.1
  • 38
    • 33745045462 scopus 로고    scopus 로고
    • + Symport by the Sucrose Permease of Escherichia coli Relative to Lactose Permease
    • DOI 10.1016/j.jmb.2006.02.050, PII S002228360600249X
    • Vadyvaloo V, Smirnova IN, Kasho VN, Kaback HR (2006) Conservation of residues involved in sugar/H(+) symport by the sucrose permease of Escherichia coli relative to lactose permease. J Mol Biol 358:1051-1059. (Pubitemid 44382450)
    • (2006) Journal of Molecular Biology , vol.358 , Issue.4 , pp. 1051-1059
    • Vadyvaloo, V.1    Smirnova, I.N.2    Kasho, V.N.3    Ronald, K.H.4
  • 40
    • 0028234751 scopus 로고
    • Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli
    • Franco PJ, Brooker RJ (1994) Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli. J Biol Chem 269:7379-7386. (Pubitemid 24217935)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.10 , pp. 7379-7386
    • Franco, P.J.1    Brooker, R.J.2
  • 41
    • 0023047638 scopus 로고
    • Lac permease of Escherichia coli: Histidine-322 and glutamic acid-325 may be components of a charge-relay system
    • Carrasco N, Antes LM, Poonian MS, Kaback HR (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
  • 44
    • 79952738070 scopus 로고    scopus 로고
    • The alternating-access mechanism of MFS transporters arises from inverted-topology repeats
    • Radestock S, Forrest LR (2011) The alternating-access mechanism of MFS transporters arises from inverted-topology repeats. J Mol Biol 407:698-715.
    • (2011) J Mol Biol , vol.407 , pp. 698-715
    • Radestock, S.1    Forrest, L.R.2
  • 45
    • 0026757193 scopus 로고
    • Possible salt bridges between transmembrane alpha-helices of the lactose carrier of Escherichia coli
    • Lee JI, Hwang PP, Hansen C, Wilson TH (1992) Possible salt bridges between transmembrane alpha-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
  • 46
    • 0026439214 scopus 로고
    • Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli
    • Sahin-Tóth M, Dunten RL, Gonzalez A, Kaback HR (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-Tóth, M.1    Dunten, R.L.2    Gonzalez, A.3    Kaback, H.R.4
  • 47
    • 0027382884 scopus 로고
    • Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli
    • DOI 10.1021/bi00089a019
    • Sahin-Tóth M, Kaback HR (1993) Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli. Biochemistry 32:10027-10035. (Pubitemid 23312429)
    • (1993) Biochemistry , vol.32 , Issue.38 , pp. 10027-10035
    • Sahin-Toth, M.1    Kaback, H.R.2
  • 48
    • 0023825249 scopus 로고
    • Bioenergetic coupling to protonmotive force: Should we be considering hydronium ion coordination and not group protonation?
    • Boyer PD (1988) Bioenergetic coupling to protonmotive force: Should we be considering hydronium ion coordination and not group protonation? Trends Biochem Sci 13:5-7.
    • (1988) Trends Biochem Sci , vol.13 , pp. 5-7
    • Boyer, P.D.1
  • 49
    • 35448959682 scopus 로고    scopus 로고
    • Two distinct proton binding sites in the ATP synthase family
    • von Ballmoos C, Dimroth P (2007) Two distinct proton binding sites in the ATP synthase family. Biochemistry 46:11800-11809.
    • (2007) Biochemistry , vol.46 , pp. 11800-11809
    • Von Ballmoos, C.1    Dimroth, P.2
  • 50
    • 0018850485 scopus 로고
    • Lactose carrier protein of Escherichia coli. Structure and expression of plasmids carrying the Y gene of the lac operon
    • Teather RM, et al. (1980) Lactose carrier protein of Escherichia coli. Structure and expression of plasmids carrying the Y gene of the lac operon. Eur J Biochem 108:223-231.
    • (1980) Eur J Biochem , vol.108 , pp. 223-231
    • Teather, R.M.1
  • 51
    • 77957010716 scopus 로고
    • Bacterial membranes
    • eds Kaplan NP, Jakoby WB, Colowick NP (Elsevier, New York)
    • Kaback HR (1971) Bacterial membranes. Methods in Enzymology, eds Kaplan NP, Jakoby WB, Colowick NP (Elsevier, New York), Vol XXII, pp 99-120.
    • (1971) Methods in Enzymology , vol.22 , pp. 99-120
    • Kaback, H.R.1
  • 52
    • 0016750458 scopus 로고
    • Localization of D-lactate dehydrogenase in native and reconstituted Escherichia coli membrane vesicles
    • Short SA, Kaback HR, Kohn LD (1975) Localization of D-lactate dehydrogenase in native and reconstituted Escherichia coli membrane vesicles. J Biol Chem 250:4291-4296.
    • (1975) J Biol Chem , vol.250 , pp. 4291-4296
    • Short, S.A.1    Kaback, H.R.2    Kohn, L.D.3


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