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Volumn 53, Issue 9, 2014, Pages 1536-1543

Galactoside-binding site in LacY

Author keywords

[No Author keywords available]

Indexed keywords

GALACTOPYRANOSIDE; HIGH- K; LACTOSE PERMEASE; MOLECULAR DYNAMICS SIMULATIONS; SIDE-CHAINS; SITE DIRECTED MUTAGENESIS; X RAY CRYSTAL STRUCTURES;

EID: 84896088314     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401716z     Document Type: Article
Times cited : (10)

References (56)
  • 2
    • 84902141845 scopus 로고    scopus 로고
    • The Life and Times of Lac Permease: Crystals Ain't Enough, but They Certainly do Help
    • In (Ziegler, C. and Kraemer, R. Eds.) Springer Series in Biophysics: Transporters, Springer, Berlin.
    • Madej, M. G. and Kaback, H. R. (2014) The Life and Times of Lac Permease: Crystals Ain't Enough, but They Certainly do Help. In Membrane transporter function: To structure and beyond (Ziegler, C. and Kraemer, R., Eds.) Springer Series in Biophysics: Transporters, Springer, Berlin.
    • (2014) Membrane Transporter Function: To Structure and beyond
    • Madej, M.G.1    Kaback, H.R.2
  • 4
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R., and Iwata, S. (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
  • 6
    • 79959349280 scopus 로고    scopus 로고
    • Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
    • Chaptal, V., Kwon, S., Sawaya, M. R., Guan, L., Kaback, H. R., and Abramson, J. (2011) Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition Proc. Natl. Acad. Sci. U.S.A. 108, 9361-9366
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9361-9366
    • Chaptal, V.1    Kwon, S.2    Sawaya, M.R.3    Guan, L.4    Kaback, H.R.5    Abramson, J.6
  • 10
    • 41649112580 scopus 로고    scopus 로고
    • Opening and closing of the periplasmic gate in lactose permease
    • Zhou, Y., Guan, L., Freites, J. A., and Kaback, H. R. (2008) Opening and closing of the periplasmic gate in lactose permease Proc. Natl. Acad. Sci. U.S.A. 105, 3774-3778
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 3774-3778
    • Zhou, Y.1    Guan, L.2    Freites, J.A.3    Kaback, H.R.4
  • 11
    • 70350553821 scopus 로고    scopus 로고
    • Residues Gating the Periplasmic Pathway of LacY
    • Zhou, Y., Nie, Y., and Kaback, H. R. (2009) Residues Gating the Periplasmic Pathway of LacY J. Mol. Biol. 394, 219-225
    • (2009) J. Mol. Biol. , vol.394 , pp. 219-225
    • Zhou, Y.1    Nie, Y.2    Kaback, H.R.3
  • 12
    • 76049089794 scopus 로고    scopus 로고
    • Probing of the rates of alternating access in LacY with Trp fluorescence
    • Smirnova, I., Kasho, V., Sugihara, J., and Kaback, H. R. (2009) Probing of the rates of alternating access in LacY with Trp fluorescence Proc. Natl. Acad. Sci. U.S.A. 106, 21561-21566
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 21561-21566
    • Smirnova, I.1    Kasho, V.2    Sugihara, J.3    Kaback, H.R.4
  • 13
    • 77953101915 scopus 로고    scopus 로고
    • Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane
    • Nie, Y. and Kaback, H. R. (2010) Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane Proc. Natl. Acad. Sci. U.S.A. 107, 9903-9908
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9903-9908
    • Nie, Y.1    Kaback, H.R.2
  • 14
    • 79952369030 scopus 로고    scopus 로고
    • Site-Directed Alkylation Studies with LacY Provide Evidence for the Alternating Access Model of Transport
    • Jiang, X., Nie, Y., and Kaback, H. R. (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
  • 15
    • 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., and Kaback, H. R. (2011) Opening the periplasmic cavity in lactose permease is the limiting step for sugar binding Proc. Natl. Acad. Sci. U.S.A. 108, 15147-15151
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 15147-15151
    • Smirnova, I.1    Kasho, V.2    Sugihara, J.3    Kaback, H.R.4
  • 17
    • 80755122853 scopus 로고    scopus 로고
    • Lactose permease and the alternating access mechanism
    • Smirnova, I., Kasho, V., and Kaback, H. R. (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
  • 18
    • 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-Tóth, M., Akhoon, K. M., Runner, J., and Kaback, H. R. (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-Tóth, M.1    Akhoon, K.M.2    Runner, J.3    Kaback, H.R.4
  • 19
    • 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
    • Sahin-Tóth, M., Lawrence, M. C., Nishio, T., and Kaback, H. R. (2001) The C-4 hydroxyl group of galactopyranosides is the major determinant for ligand recognition by the lactose permease of Escherichia coli Biochemistry 40, 13015-13019
    • (2001) Biochemistry , vol.40 , pp. 13015-13019
    • Sahin-Tóth, M.1    Lawrence, M.C.2    Nishio, T.3    Kaback, H.R.4
  • 20
    • 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
    • Frillingos, S., Gonzalez, A., and Kaback, H. R. (1997) Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential Biochemistry 36, 14284-14290
    • (1997) Biochemistry , vol.36 , pp. 14284-14290
    • Frillingos, S.1    Gonzalez, A.2    Kaback, H.R.3
  • 21
    • 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-Toth, M., le Coutre, J., Kharabi, D., le Maire, G., Lee, J. C., and Kaback, H. R. (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-Toth, M.1    Le Coutre, J.2    Kharabi, D.3    Le Maire, G.4    Lee, J.C.5    Kaback, H.R.6
  • 22
    • 0032544066 scopus 로고    scopus 로고
    • The substrate-binding site in the lactose permease of Escherichia coli
    • Venkatesan, P. and Kaback, H. R. (1998) The substrate-binding site in the lactose permease of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 95, 9802-9807
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9802-9807
    • Venkatesan, P.1    Kaback, H.R.2
  • 23
    • 0034705079 scopus 로고    scopus 로고
    • Thiol cross-linking of transmembrane domains IV and v in the lactose permease of Escherichia coli
    • Wolin, C. D. and Kaback, H. R. (2000) Thiol cross-linking of transmembrane domains IV and V in the lactose permease of Escherichia coli Biochemistry 39, 6130-6135
    • (2000) Biochemistry , vol.39 , pp. 6130-6135
    • Wolin, C.D.1    Kaback, H.R.2
  • 24
    • 0037452555 scopus 로고    scopus 로고
    • Aromatic stacking in the sugar binding site of the lactose permease
    • Guan, L., Hu, Y., and Kaback, H. R. (2003) Aromatic stacking in the sugar binding site of the lactose permease Biochemistry 42, 1377-1382
    • (2003) Biochemistry , vol.42 , pp. 1377-1382
    • Guan, L.1    Hu, Y.2    Kaback, H.R.3
  • 25
    • 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
    • Vazquez-Ibar, J. L., Guan, L., Svrakic, M., and Kaback, H. R. (2003) Exploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 100, 12706-12711
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12706-12711
    • Vazquez-Ibar, J.L.1    Guan, L.2    Svrakic, M.3    Kaback, H.R.4
  • 26
    • 0028313224 scopus 로고
    • Role of glutamate-269 in the lactose permease of Escherichia coli
    • Ujwal, M. L., Sahin-Toth, M., Persson, B., and Kaback, H. R. (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
  • 27
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure function relationships in polytopic membrane proteins
    • Frillingos, S., Sahin-Toth, M., Wu, J., and Kaback, H. R. (1998) Cys-scanning mutagenesis: A novel approach to structure function relationships in polytopic membrane proteins FASEB J. 12, 1281-1299
    • (1998) FASEB J. , vol.12 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Toth, M.2    Wu, J.3    Kaback, H.R.4
  • 28
    • 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
    • He, M. M. and Kaback, H. R. (1997) Interaction between residues Glu269 (helix VIII) and His322 (helix X) of the lactose permease of Escherichia coli is essential for substrate binding Biochemistry 36, 13688-13692
    • (1997) Biochemistry , vol.36 , pp. 13688-13692
    • He, M.M.1    Kaback, H.R.2
  • 30
    • 0344838440 scopus 로고    scopus 로고
    • Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry
    • Weinglass, A. B., Whitelegge, J. P., Hu, Y., Verner, G. E., Faull, K. F., and Kaback, H. R. (2003) Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry EMBO J. 22, 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
  • 31
    • 0031056670 scopus 로고    scopus 로고
    • The role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis
    • Frillingos, S., Ujwal, M. L., Sun, J., and Kaback, H. R. (1997) The role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis Protein Sci. 6, 431-437
    • (1997) Protein Sci. , vol.6 , pp. 431-437
    • Frillingos, S.1    Ujwal, M.L.2    Sun, J.3    Kaback, H.R.4
  • 32
    • 0030614685 scopus 로고    scopus 로고
    • The role of helix VIII in the lactose permease of Escherichia coli: II. Site-directed sulfhydryl modification
    • Frillingos, S. and Kaback, H. R. (1997) The role of helix VIII in the lactose permease of Escherichia coli: II. Site-directed sulfhydryl modification Protein Sci. 6, 438-443
    • (1997) Protein Sci. , vol.6 , pp. 438-443
    • Frillingos, S.1    Kaback, H.R.2
  • 34
    • 82555176541 scopus 로고    scopus 로고
    • MATCH: An atom-typing toolset for molecular mechanics force fields
    • Yesselman, J. D., Price, D. J., Knight, J. L., and Brooks, C. L., III (2012) MATCH: An atom-typing toolset for molecular mechanics force fields J. Comput. Chem. 33, 189-202
    • (2012) J. Comput. Chem. , vol.33 , pp. 189-202
    • Yesselman, J.D.1    Price, D.J.2    Knight, J.L.3    Brooks III, C.L.4
  • 38
  • 39
    • 84963146276 scopus 로고
    • Generalized Verlet Algorithm for Efficient Molecular Dynamics Simulations with Long-range Interactions
    • Grubmüller, H., Heller, H., Windemuth, A., and Schulten, K. (1991) Generalized Verlet Algorithm for Efficient Molecular Dynamics Simulations with Long-range Interactions Mol. Simul. 6, 121-142
    • (1991) Mol. Simul. , vol.6 , pp. 121-142
    • Grubmüller, H.1    Heller, H.2    Windemuth, A.3    Schulten, K.4
  • 40
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 42
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.-P., Ciccotti, G., and Berendsen, H. (1977) Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes J. Comput. Phys. 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.3
  • 43
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • Miyamoto, S. and Kollman, P. (1992) Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models J. Comput. Chem. 13, 952-962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.2
  • 44
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller, S., Zhang, Y., Pastor, R., and Brooks, B. (1995) Constant pressure molecular dynamics simulation: The Langevin piston method J. Chem. Phys. 103, 4613-4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.1    Zhang, Y.2    Pastor, R.3    Brooks, B.4
  • 45
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • Martyna, G., Tobias, D., and Klein, M. (1994) Constant pressure molecular dynamics algorithms J. Chem. Phys. 101, 4177-4189
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.1    Tobias, D.2    Klein, M.3
  • 47
    • 0018850485 scopus 로고
    • Lactose carrier protein of Escherichia coli. Structure and expression of plasmids carrying the Y-gene of the lac operon
    • Teather, R. M., Bramhall, J., Riede, I., Wright, J. K., Furst, M., Aichele, G., Wilhelm, U., and Overath, P. (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    Bramhall, J.2    Riede, I.3    Wright, J.K.4    Furst, M.5    Aichele, G.6    Wilhelm, U.7    Overath, P.8
  • 48
    • 0017839043 scopus 로고
    • Amplification of the lactose carrier protein in Escherichia coli using a plasmid vector
    • Teather, R. M., Müller-Hill, B., Abrutsch, U., Aichele, G., and Overath, P. (1978) Amplification of the lactose carrier protein in Escherichia coli using a plasmid vector Mol. Gen. Genet. 159, 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
  • 49
    • 0016321695 scopus 로고
    • Transport in isolated bacterial membrane vesicles
    • Kaback, H. R. (1974) Transport in isolated bacterial membrane vesicles Methods Enzymol. 31, 698-709
    • (1974) Methods Enzymol. , vol.31 , pp. 698-709
    • Kaback, H.R.1
  • 50
    • 0037452911 scopus 로고    scopus 로고
    • A mutation in the lactose permease of Escherichia coli that decreases conformational flexibility and increases protein stability
    • Smirnova, I. N. and Kaback, H. R. (2003) A mutation in the lactose permease of Escherichia coli that decreases conformational flexibility and increases protein stability Biochemistry 42, 3025-3031
    • (2003) Biochemistry , vol.42 , pp. 3025-3031
    • Smirnova, I.N.1    Kaback, H.R.2
  • 52
    • 33845945208 scopus 로고    scopus 로고
    • Direct Sugar Binding to LacY Measured by Resonance Energy Transfer
    • Smirnova, I. N., Kasho, V. N., and Kaback, H. R. (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
  • 53
    • 0037076369 scopus 로고    scopus 로고
    • Changing the lactose permease of Escherichia coli into a galactose-specific symporter
    • Guan, L., Sahin-Toth, M., and Kaback, H. R. (2002) Changing the lactose permease of Escherichia coli into a galactose-specific symporter Proc. Natl. Acad. Sci. U.S.A. 99, 6613-6618
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6613-6618
    • Guan, L.1    Sahin-Toth, M.2    Kaback, H.R.3
  • 54
    • 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
    • Robertson, D. E., Kaczorowski, G. J., Garcia, M. L., and Kaback, H. R. (1980) 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, 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
  • 55
    • 0037195244 scopus 로고    scopus 로고
    • Binding of hydrophobic d -galactopyranosides to the lactose permease of Escherichia coli
    • Sahin-Tóth, M., Gunawan, P., Lawrence, M. C., Toyokuni, T., and Kaback, H. R. (2002) Binding of hydrophobic d -galactopyranosides to the lactose permease of Escherichia coli Biochemistry 41, 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
  • 56
    • 33745034030 scopus 로고    scopus 로고
    • Sequence alignment and homology threading reveals prokaryotic and eukaryotic proteins similar to lactose permease
    • Kasho, V. N., Smirnova, I. N., and Kaback, H. R. (2006) Sequence alignment and homology threading reveals prokaryotic and eukaryotic proteins similar to lactose permease J. Mol. Biol. 358, 1060-1070
    • (2006) J. Mol. Biol. , vol.358 , pp. 1060-1070
    • Kasho, V.N.1    Smirnova, I.N.2    Kaback, H.R.3


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