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Volumn 406, Issue 1, 2011, Pages 59-74

Homology model of the Na+/proline transporter PutP of Escherichia coli and its functional implications

Author keywords

docking; molecular modeling; PutP; secondary transport; sodium solute symport

Indexed keywords

COTRANSPORTER; COTRANSPORTER PUTP; COTRANSPORTER SGLT; PROLINE; SODIUM ION; UNCLASSIFIED DRUG;

EID: 79151480337     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.11.045     Document Type: Article
Times cited : (22)

References (44)
  • 1
    • 0037010179 scopus 로고    scopus 로고
    • The sodium/substrate symporter family: Structural and functional features
    • Jung H. The sodium/substrate symporter family: structural and functional features FEBS Lett. 529 2002 73 77
    • (2002) FEBS Lett. , vol.529 , pp. 73-77
    • Jung, H.1
  • 2
    • 1242272759 scopus 로고    scopus 로고
    • The sodium/glucose cotransport family SLC5
    • Wright E.M., and Turk E. The sodium/glucose cotransport family SLC5 Pflugers Arch. 447 2004 510 518
    • (2004) Pflugers Arch. , vol.447 , pp. 510-518
    • Wright, E.M.1    Turk, E.2
  • 3
    • 0028239439 scopus 로고
    • A functional superfamily of sodium/solute symporters
    • Reizer J., Reizer A., and Saier M.H. Jr. A functional superfamily of sodium/solute symporters Biochim. Biophys. Acta 1197 1994 133 166
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 133-166
    • Reizer, J.1    Reizer, A.2    Saier Jr., M.H.3
  • 4
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O. Simple allosteric model for membrane pumps Nature 211 1966 969 970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 5
    • 0031458238 scopus 로고    scopus 로고
    • Ligand conduction and the gated-pore mechanism of transmembrane transport
    • West I.C. Ligand conduction and the gated-pore mechanism of transmembrane transport Bioch. Biophys. Acta 1331 1997 213 234
    • (1997) Bioch. Biophys. Acta , vol.1331 , pp. 213-234
    • West, I.C.1
  • 6
    • 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. Probing of the rates of alternating access in LacY with Trp fluorescence Proc. Natl Acad. Sci. USA 106 2009 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
  • 7
    • 77951585158 scopus 로고    scopus 로고
    • Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1
    • Shimamura T., Weyand S., Beckstein O., Rutherford N.G., Hadden J.M., and Sharples D. Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1 Science 328 2010 470 473
    • (2010) Science , vol.328 , pp. 470-473
    • Shimamura, T.1    Weyand, S.2    Beckstein, O.3    Rutherford, N.G.4    Hadden, J.M.5    Sharples, D.6
  • 9
    • 34247248894 scopus 로고    scopus 로고
    • Secondary transport of amino acids in prokaryotes
    • Jung H., Pirch T., and Hilger D. Secondary transport of amino acids in prokaryotes J. Membr. Biol. 213 2006 119 133
    • (2006) J. Membr. Biol. , vol.213 , pp. 119-133
    • Jung, H.1    Pirch, T.2    Hilger, D.3
  • 17
    • 0023687818 scopus 로고
    • Mitochondrial targeting sequences. Why 'non-amphiphilic' peptides may still be amphiphilic
    • Gavel Y., Nilsson L., and von Heijne G. Mitochondrial targeting sequences. Why 'non-amphiphilic' peptides may still be amphiphilic FEBS Lett. 235 1988 173 177
    • (1988) FEBS Lett. , vol.235 , pp. 173-177
    • Gavel, Y.1    Nilsson, L.2    Von Heijne, G.3
  • 18
    • 0242290359 scopus 로고    scopus 로고
    • +/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane
    • +/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane J. Biol. Chem. 278 2003 42942 42949
    • (2003) J. Biol. Chem. , vol.278 , pp. 42942-42949
    • Pirch, T.1    Landmeier, S.2    Jung, H.3
  • 20
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • Landau M., Mayrose I., Rosenberg Y., Glaser F., Martz E., Pupko T., and Ben-Tal N. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures Nucleic Acids Res. 33 2005 W299 302
    • (2005) Nucleic Acids Res. , vol.33 , pp. 299-302
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7
  • 21
    • 41949124711 scopus 로고    scopus 로고
    • +/proline transporter PutP of Escherichia coli in ligand binding and transport
    • +/proline transporter PutP of Escherichia coli in ligand binding and transport J. Biol. Chem. 283 2008 4921 4929
    • (2008) J. Biol. Chem. , vol.283 , pp. 4921-4929
    • Hilger, D.1    Böhm, M.2    Hackmann, A.3    Jung, H.4
  • 22
    • 72249106725 scopus 로고    scopus 로고
    • Ion-releasing state of a secondary membrane transporter
    • Li J., and Tajkhorshid E. Ion-releasing state of a secondary membrane transporter Biophys. J. 97 2009 L29 L31
    • (2009) Biophys. J. , vol.97
    • Li, J.1    Tajkhorshid, E.2
  • 23
    • 0030887995 scopus 로고    scopus 로고
    • +-coupled proline uptake
    • +-coupled proline uptake Biochemistry 36 1997 4631 4636
    • (1997) Biochemistry , vol.36 , pp. 4631-4636
    • Quick, M.1    Jung, H.2
  • 26
    • 0037044743 scopus 로고    scopus 로고
    • The transmembrane domains of the ABC multidrug transporter LmrA form a cytoplasmic exposed, aqueous chamber within the membrane
    • Poelarends G., and Konings W.N. The transmembrane domains of the ABC multidrug transporter LmrA form a cytoplasmic exposed, aqueous chamber within the membrane J. Biol. Chem. 277 2002 42891 42898
    • (2002) J. Biol. Chem. , vol.277 , pp. 42891-42898
    • Poelarends, G.1    Konings, W.N.2
  • 27
    • 34548156802 scopus 로고    scopus 로고
    • Site-directed alkylation of cysteine to test solvent accessibility of membrane proteins
    • Guan L., and Kaback H.R. Site-directed alkylation of cysteine to test solvent accessibility of membrane proteins Nat. Protoc. 2 2007 2012 2017
    • (2007) Nat. Protoc. , vol.2 , pp. 2012-2017
    • Guan, L.1    Kaback, H.R.2
  • 29
    • 55349092991 scopus 로고    scopus 로고
    • Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter
    • Weyand S., Shimamura T., Yajima S., Suzuki S. i., Mirza O., and Krusong K. Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter Science 322 2008 709 713
    • (2008) Science , vol.322 , pp. 709-713
    • Weyand, S.1    Shimamura, T.2    Yajima, S.3    S, S.I.4    Mirza, O.5    Krusong, K.6
  • 32
    • 77952481518 scopus 로고    scopus 로고
    • The sodium/galactose symporter crystal structure is a dynamic, not so occluded state
    • Zomot E., and Bahar I. The sodium/galactose symporter crystal structure is a dynamic, not so occluded state Mol. Biosyst. 6 2010 1040 1046
    • (2010) Mol. Biosyst. , vol.6 , pp. 1040-1046
    • Zomot, E.1    Bahar, I.2
  • 33
    • 0029957853 scopus 로고    scopus 로고
    • Ser57 in the Na+/proline permease of Escherichia coli is critical for high-affinity proline uptake
    • Quick M., Tebbe S., and Jung H. Ser57 in the Na+/proline permease of Escherichia coli is critical for high-affinity proline uptake Eur. J. Biochem. 239 1996 732 736
    • (1996) Eur. J. Biochem. , vol.239 , pp. 732-736
    • Quick, M.1    Tebbe, S.2    Jung, H.3
  • 34
    • 0035910390 scopus 로고    scopus 로고
    • Neutralization of a conserved amino acid residue in the human Na+/glucose transporter (hSGLT1) generates a glucose-gated H+ channel
    • Quick M., Loo D.D., and Wright E.M. Neutralization of a conserved amino acid residue in the human Na+/glucose transporter (hSGLT1) generates a glucose-gated H+ channel J. Biol. Chem. 276 2001 1728 1734
    • (2001) J. Biol. Chem. , vol.276 , pp. 1728-1734
    • Quick, M.1    Loo, D.D.2    Wright, E.M.3
  • 36
    • 12144289984 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • Friesner R.A., Banks J.L., Murphy R.B., Halgren T.A., Klicic J.J., and Mainz D.T. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy J. Med. Chem. 47 2004 1739 1749
    • (2004) J. Med. Chem. , vol.47 , pp. 1739-1749
    • Friesner, R.A.1    Banks, J.L.2    Murphy, R.B.3    Halgren, T.A.4    Klicic, J.J.5    Mainz, D.T.6
  • 37
    • 33750124980 scopus 로고    scopus 로고
    • Extra precision glide: Docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes
    • Friesner R.A., Murphy R.B., Repasky M.P., Frye L.L., Greenwood J.R., and Halgren T.A. Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes J. Med. Chem. 49 2006 6177 6196
    • (2006) J. Med. Chem. , vol.49 , pp. 6177-6196
    • Friesner, R.A.1    Murphy, R.B.2    Repasky, M.P.3    Frye, L.L.4    Greenwood, J.R.5    Halgren, T.A.6
  • 38
    • 67651002876 scopus 로고    scopus 로고
    • Energetic analysis of fragment docking and application to structure-based pharmacophore hypothesis generation
    • Loving K., Salam N., and Sherman W. Energetic analysis of fragment docking and application to structure-based pharmacophore hypothesis generation J. Comput. Aided Mol. Des. 23 2009 541 554
    • (2009) J. Comput. Aided Mol. Des. , vol.23 , pp. 541-554
    • Loving, K.1    Salam, N.2    Sherman, W.3
  • 39
    • 0021031927 scopus 로고
    • Two proline porters in Escherichia coli K-12
    • Stalmach M.E., Grothe S., and Wood J.M. Two proline porters in Escherichia coli K-12 J. Bacteriol. 156 1983 481 486
    • (1983) J. Bacteriol. , vol.156 , pp. 481-486
    • Stalmach, M.E.1    Grothe, S.2    Wood, J.M.3
  • 40
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor S., and Richardson C.C. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes Proc. Natl Acad. Sci. USA 82 1985 1074 1078
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 41
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann E., Ochs B., and Abel K.J. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli Gene 69 1988 301 315
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 43
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 44
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable Anal. Biochem. 83 1977 346 356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.