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Volumn 110, Issue 28, 2013, Pages 11343-11348

Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT

Author keywords

Membrane transporter; Molecular dynamics simulation; X ray crystallography

Indexed keywords

ALAFOSFALIN; GLUTAMIC ACID; PEPTIDE TRANSPORTER 1; PROTON DEPENDENT OLIGOPEPTIDE TRANSPORTER; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 84879895875     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1301079110     Document Type: Article
Times cited : (157)

References (38)
  • 1
    • 84874258738 scopus 로고    scopus 로고
    • Structural advances for the major facilitator superfamily (MFS) transporters
    • Yan N (2013) Structural advances for the major facilitator superfamily (MFS) transporters. Trends Biochem Sci 38(3):151-159.
    • (2013) Trends Biochem Sci , vol.38 , Issue.3 , pp. 151-159
    • Yan, N.1
  • 4
    • 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(51):21561-21566.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.51 , pp. 21561-21566
    • Smirnova, I.1    Kasho, V.2    Sugihara, J.3    Kaback, H.R.4
  • 5
    • 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(5):698-715.
    • (2011) J Mol Biol , vol.407 , Issue.5 , pp. 698-715
    • Radestock, S.1    Forrest, L.R.2
  • 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(5633):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(6):1177-1183.
    • (2006) EMBO J , vol.25 , Issue.6 , pp. 1177-1183
    • Mirza, O.1    Guan, L.2    Verner, G.3    Iwata, S.4    Kaback, H.R.5
  • 9
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • DOI 10.1126/science.1087619
    • Huang YF, Lemieux MJ, Song JM, Auer M, Wang DN (2003) Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301(5633):616-620. (Pubitemid 36927940)
    • (2003) Science , vol.301 , Issue.5633 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.-N.5
  • 10
    • 84876797248 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic phosphate transporter
    • Pedersen BP, et al. (2013) Crystal structure of a eukaryotic phosphate transporter. Nature 496(7446):533-536.
    • (2013) Nature , vol.496 , Issue.7446 , pp. 533-536
    • Pedersen, B.P.1
  • 11
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin Y, He X, Szewczyk P, Nguyen T, Chang G (2006) Structure of the multidrug transporter EmrD from Escherichia coli. Science 312(5774):741-744.
    • (2006) Science , vol.312 , Issue.5774 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 12
    • 84875810015 scopus 로고    scopus 로고
    • Structure and mechanism of a nitrate transporter
    • Yan H, et al. (2013) Structure and mechanism of a nitrate transporter. Cell Rep 3(3):716-723.
    • (2013) Cell Rep , vol.3 , Issue.3 , pp. 716-723
    • Yan, H.1
  • 13
    • 84867657593 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of glucose transporters GLUT1-4
    • Sun LF, et al. (2012) Crystal structure of a bacterial homologue of glucose transporters GLUT1-4. Nature 490(7420):361-366.
    • (2012) Nature , vol.490 , Issue.7420 , pp. 361-366
    • Sun, L.F.1
  • 14
    • 77958010505 scopus 로고    scopus 로고
    • Structure of a fucose transporter in an outward-open conformation
    • Dang SY, et al. (2010) Structure of a fucose transporter in an outward-open conformation. Nature 467(7316):734-738.
    • (2010) Nature , vol.467 , Issue.7316 , pp. 734-738
    • Dang, S.Y.1
  • 15
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • Forrest LR, Kramer R, Ziegler C (2011) The structural basis of secondary active transport mechanisms. Biochim. Biophys. Acta-Bioenerg. 1807(2):167-188.
    • (2011) Biochim. Biophys. Acta-Bioenerg. , vol.1807 , Issue.2 , pp. 167-188
    • Forrest, L.R.1    Kramer, R.2    Ziegler, C.3
  • 16
    • 0028151656 scopus 로고
    • The POT family of transport proteins
    • DOI 10.1016/0968-0004(94)90087-6
    • Paulsen IT, Skurray RA (1994) The POT family of transport proteins. Trends Biochem Sci 19(10):404. (Pubitemid 24320128)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.10 , pp. 404
    • Paulsen, I.T.1    Skurray, R.A.2
  • 17
    • 0029144324 scopus 로고
    • The PTR family: A new group of peptide transporters
    • Steiner HY, Naider F, Becker JM (1995) The PTR family: a new group of peptide transporters. Mol Microbiol 16(5):825-834.
    • (1995) Mol Microbiol , vol.16 , Issue.5 , pp. 825-834
    • Steiner, H.Y.1    Naider, F.2    Becker, J.M.3
  • 18
    • 0021025978 scopus 로고
    • Role of pH gradient and membrane potential in dipeptide transport in intestinal and renal brush-border membrane vesicles from the rabbit. Studies with L-carnosine and glycyl-L-proline
    • Ganapathy V, Leibach FH (1983) Role of pH gradient and membrane potential in dipeptide transport in intestinal and renal brush-border membrane vesicles from the rabbit. Studies with L-carnosine and glycyl-L-proline. J Biol Chem 258(23):14189-14192. (Pubitemid 14217939)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.23 , pp. 14189-14192
    • Ganapathy, V.1    Leibach, F.H.2
  • 19
    • 33646720881 scopus 로고    scopus 로고
    • From bacteria to man: Archaic proton-dependent peptide transporters at work
    • DOI 10.1152/physiol.00054.2005
    • Daniel H, Spanier B, Kottra G, Weitz D (2006) From bacteria to man: archaic protondependent peptide transporters at work. Physiology (Bethesda) 21:93-102. (Pubitemid 43752505)
    • (2006) Physiology , vol.21 , Issue.2 , pp. 93-102
    • Daniel, H.1    Spanier, B.2    Kottra, G.3    Weitz, D.4
  • 20
    • 0028333611 scopus 로고
    • Expression cloning of a mammalian proton-coupled oligopeptide transporter
    • Fei YJ, et al. (1994) Expression cloning of a mammalian proton-coupled oligopeptide transporter. Nature 368(6471):563-566.
    • (1994) Nature , vol.368 , Issue.6471 , pp. 563-566
    • Fei, Y.J.1
  • 21
    • 0032573036 scopus 로고    scopus 로고
    • Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions
    • DOI 10.1021/bi981128k
    • Covitz KMY, Amidon GL, Sadée W (1998) Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions. Biochemistry 37(43):15214-15221. (Pubitemid 28503250)
    • (1998) Biochemistry , vol.37 , Issue.43 , pp. 15214-15221
    • Covitz, K.-M.Y.1    Amidon, G.L.2    Sadee, W.3
  • 22
    • 84873329542 scopus 로고    scopus 로고
    • Proton-coupled oligopeptide transporter family SLC15: Physiological, pharmacological and pathological implications
    • Smith DE, Clémençon B, Hediger MA (2013) Proton-coupled oligopeptide transporter family SLC15: physiological, pharmacological and pathological implications. Mol Aspects Med 34(2-3):323-336.
    • (2013) Mol Aspects Med , vol.34 , Issue.2-3 , pp. 323-336
    • Smith, D.E.1    Clémençon, B.2    Hediger, M.A.3
  • 23
    • 0028840804 scopus 로고
    • Stereoselective uptake of beta-lactam antibiotics by the intestinal peptide transporter
    • Wenzel U, Thwaites DT, Daniel H (1995) Stereoselective uptake of beta-lactam antibiotics by the intestinal peptide transporter. Br J Pharmacol 116(7):3021-3027.
    • (1995) Br J Pharmacol , vol.116 , Issue.7 , pp. 3021-3027
    • Wenzel, U.1    Thwaites, D.T.2    Daniel, H.3
  • 25
    • 13944269270 scopus 로고    scopus 로고
    • A novel high-throughput pepT1 transporter assay differentiates between substrates and antagonists
    • Faria TN, et al. (2004) A novel high-throughput pepT1 transporter assay differentiates between substrates and antagonists. Mol Pharm 1(1):67-76.
    • (2004) Mol Pharm , vol.1 , Issue.1 , pp. 67-76
    • Faria, T.N.1
  • 27
    • 78751604619 scopus 로고    scopus 로고
    • Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2
    • Newstead S, et al. (2011) Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2. EMBO J 30(2):417-426.
    • (2011) EMBO J , vol.30 , Issue.2 , pp. 417-426
    • Newstead, S.1
  • 28
    • 84865237281 scopus 로고    scopus 로고
    • Alternating access mechanism in the POT family of oligopeptide transporters
    • Solcan N, et al. (2012) Alternating access mechanism in the POT family of oligopeptide transporters. EMBO J 31(16):3411-3421.
    • (2012) EMBO J , vol.31 , Issue.16 , pp. 3411-3421
    • Solcan, N.1
  • 29
    • 44949101288 scopus 로고    scopus 로고
    • DtpB (YhiP) and DtpA (TppB, YdgR) are prototypical proton-dependent peptide transporters of Escherichia coli
    • DOI 10.1111/j.1742-4658.2008.06477.x
    • Harder D, et al. (2008) DtpB (YhiP) and DtpA (TppB, YdgR) are prototypical protondependent peptide transporters of Escherichia coli. FEBS J 275(13):3290-3298. (Pubitemid 351813542)
    • (2008) FEBS Journal , vol.275 , Issue.13 , pp. 3290-3298
    • Harder, D.1    Stolz, J.2    Casagrande, F.3    Obrdlik, P.4    Weitz, D.5    Fotiadis, D.6    Daniel, H.7
  • 31
    • 2442688922 scopus 로고    scopus 로고
    • +/peptide cotransporters PEPT1 and PEPT2 in intestinal and renal epithelial cells
    • DOI 10.1111/j.1432-1033.2004.04114.x
    • Neumann J, Bruch M, Gebauer S, Brandsch M (2004) Transport of the phosphonodipeptide alafosfalin by the H+/peptide cotransporters PEPT1 and PEPT2 in intestinal and renal epithelial cells. Eur J Biochem 271(10):2012-2017. (Pubitemid 38657353)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.10 , pp. 2012-2017
    • Neumann, J.1    Bruch, M.2    Gebauer, S.3    Brandsch, M.4
  • 32
    • 69949127756 scopus 로고    scopus 로고
    • Mutagenesis and cysteine scanning of transmembrane domain 10 of the human dipeptide transporter
    • Xu LY, Haworth IS, Kulkarni AA, Bolger MB, Davies DL (2009) Mutagenesis and cysteine scanning of transmembrane domain 10 of the human dipeptide transporter. Pharm Res 26(10):2358-2366.
    • (2009) Pharm Res , vol.26 , Issue.10 , pp. 2358-2366
    • Xu, L.Y.1    Haworth, I.S.2    Kulkarni, A.A.3    Bolger, M.B.4    Davies, D.L.5
  • 33
    • 0034004725 scopus 로고    scopus 로고
    • Kinetics and substrate specificity of membrane-reconstituted peptide transporter DtpT of Lactococcus lactis
    • DOI 10.1128/JB.182.9.2530-2535.2000
    • Fang G, Konings WN, Poolman B (2000) Kinetics and substrate specificity of mem-brane- reconstituted peptide transporter DtpT of Lactococcus lactis. J Bacteriol 182(9):2530-2535. (Pubitemid 30212912)
    • (2000) Journal of Bacteriology , vol.182 , Issue.9 , pp. 2530-2535
    • Fang, G.1    Konings, W.N.2    Poolman, B.3
  • 34
    • 33845380397 scopus 로고    scopus 로고
    • Sugar binding and protein conformational changes in lactose permease
    • DOI 10.1529/biophysj.106.085993
    • Yin Y, Jensen MO, Tajkhorshid E, Schulten K (2006) Sugar binding and protein conformational changes in lactose permease. Biophys J 91(11):3972-3985. (Pubitemid 44889188)
    • (2006) Biophysical Journal , vol.91 , Issue.11 , pp. 3972-3985
    • Yin, Y.1    Jensen, M.O.2    Tajkhorshid, E.3    Schulten, K.4
  • 35
    • 34447256364 scopus 로고    scopus 로고
    • Conformational Change in an MFS Protein: MD Simulations of LacY
    • DOI 10.1016/j.str.2007.06.004, PII S0969212607002092
    • Holyoake J, Sansom MSP (2007) Conformational change in an MFS protein: MD simulations of LacY. Structure 15(7):873-884. (Pubitemid 47042433)
    • (2007) Structure , vol.15 , Issue.7 , pp. 873-884
    • Holyoake, J.1    Sansom, M.S.P.2
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50(Pt 5):760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763


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