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Volumn 42, Issue 1, 2013, Pages 51-72

Common folds and transport mechanisms of secondary active transporters

Author keywords

alternating access; carrier; membrane transporter; secondary active transporter; transport mechanism; transporter fold

Indexed keywords

ABC TRANSPORTER; ADIC PROTEIN; CARRIER PROTEIN; LEUT PROTEIN; MEMBRANE PROTEIN; MHP1 PROTEIN; NHAA PROTEIN; SECONDARY ACTIVE TRANSPORTER; UNCLASSIFIED DRUG; VSGLT PROTEIN;

EID: 84874249804     PISSN: 1936122X     EISSN: 19361238     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-083012-130429     Document Type: Article
Times cited : (230)

References (106)
  • 2
    • 69249136609 scopus 로고    scopus 로고
    • Structure and function of Na+-symporters with inverted repeats
    • Abramson J,Wright EM. 2009. Structure and function of Na+-symporters with inverted repeats. Curr. Opin. Struct. Biol. 19:425-322
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 425-322
    • Abramson, J.1    Wright, E.M.2
  • 3
    • 1542288949 scopus 로고    scopus 로고
    • Secondary active transport mediated by a prokaryotic homologue of ClC Cl channels
    • Accardi A, Miller C. 2004. Secondary active transport mediated by a prokaryotic homologue of ClC Cl channels. Nature 427:803-77
    • (2004) Nature , vol.427 , pp. 803-877
    • Accardi, A.1    Miller, C.2
  • 4
    • 33644536712 scopus 로고    scopus 로고
    • The aquaporin water channels
    • Agre P. 2006. The aquaporin water channels. Proc. Am. Thorac. Soc. 3:5-133
    • (2006) Proc. Am. Thorac. Soc , vol.3 , pp. 5-133
    • Agre, P.1
  • 5
    • 63449139456 scopus 로고    scopus 로고
    • Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding
    • Aller SG, Yu J, Ward A, Weng Y, Chittaboina S, et al. 2009. Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding. Science 323:1718-222
    • (2009) Science , vol.323 , pp. 1718-1232
    • Aller, S.G.1    Yu, J.2    Ward, A.3    Weng, Y.4    Chittaboina, S.5
  • 6
    • 0015829131 scopus 로고
    • The asymmetry of the facilitated transfer system for hexoses in human red cells and the simple kinetics of a two component model
    • Baker GF, Widdas WF. 1973. The asymmetry of the facilitated transfer system for hexoses in human red cells and the simple kinetics of a two component model. J. Physiol. 231:143-655
    • (1973) J. Physiol , vol.231 , pp. 143-655
    • Baker, G.F.1    Widdas, W.F.2
  • 7
    • 84857690224 scopus 로고    scopus 로고
    • 3D ultrastructure of the nuclear pore complex
    • Bilokapic S, Schwartz TU. 2012. 3D ultrastructure of the nuclear pore complex. Curr. Opin. Cell Biol. 24:86-911
    • (2012) Curr. Opin. Cell Biol , Issue.24 , pp. 86-911
    • Bilokapic, S.1    Schwartz, T.U.2
  • 8
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, et al. 1997. The complete genome sequence of Escherichia coli K-12. Science 277:1453-622
    • (1997) Science , vol.277 , pp. 1453-1622
    • Blattner, F.R.1    Bloch, C.A.2    Perna, N.T.3    Burland, V.4
  • 9
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker O, Ryan RM, Yernool D, Shimamoto K, Gouaux E. 2007. Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445:387-933
    • (2007) Nature , vol.445 , pp. 387-933
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 10
    • 84856244292 scopus 로고    scopus 로고
    • Crystal structure of the human k2p traak a lipidand mechano-sensitive k+ ion channel
    • Brohawn SG, delMarmol J,MacKinnon R. 2012. Crystal structure of the human K2P TRAAK, a lipidand mechano-sensitive K+ ion channel. Science 335:436-411
    • (2012) Science , vol.335 , pp. 436-411
    • Brohawn, S.G.1    Delmarmol, J.2    MacKinnon, R.3
  • 11
  • 12
    • 84865138166 scopus 로고    scopus 로고
    • Membrane protein structure determination using crystallography and lipidic mesophases: Recent advances and successes
    • Caffrey M, Li D, Dukkipati A. 2012. Membrane protein structure determination using crystallography and lipidic mesophases: Recent advances and successes. Biochemistry 51:6266-888
    • (2012) Biochemistry , vol.51 , pp. 6266-6888
    • Caffrey, M.1    Li, D.2    Dukkipati, A.3
  • 13
    • 0021736230 scopus 로고
    • Human erythrocyte hexose transporter activity is governed by bilayer lipid composition in reconstituted vesicles
    • Carruthers A, Melchior DL. 1984. Human erythrocyte hexose transporter activity is governed by bilayer lipid composition in reconstituted vesicles. Biochemistry 23:6901-111
    • (1984) Biochemistry , vol.23 , pp. 6901-6121
    • Carruthers, A.1    Melchior, D.L.2
  • 17
    • 0021280174 scopus 로고
    • Purification of the calcium antagonist receptor of the voltage-sensitive calcium channel from skeletal muscle transverse tubules
    • Curtis BM, Catterall WA. 1984. Purification of the calcium antagonist receptor of the voltage-sensitive calcium channel from skeletal muscle transverse tubules. Biochemistry 23:2113-188
    • (1984) Biochemistry , vol.23 , pp. 2113-2188
    • Curtis, B.M.1    Catterall, W.A.2
  • 18
    • 77958010505 scopus 로고    scopus 로고
    • Structure of a fucose transporter in an outward-open conformation
    • Dang S, Sun L, Huang Y, Lu F, Liu Y, et al. 2010. Structure of a fucose transporter in an outward-open conformation. Nature 467:734-388
    • (2010) Nature , vol.467 , pp. 734-388
    • Dang, S.1    Sun, L.2    Huang, Y.3    Lu, F.4    Liu, Y.5
  • 19
    • 35648963623 scopus 로고    scopus 로고
    • ABC transporters: How small machines do a big job
    • Davidson AL,Maloney PC. 2007. ABC transporters: How small machines do a big job. Trends Microbiol. 15:448-555
    • (2007) Trends Microbiol , vol.15 , pp. 448-555
    • Davidson, A.L.1    Maloney, P.C.2
  • 20
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 ̊a resolution
    • Deisenhofer J, Epp O, Miki K, Huber R, Michel H. 1985. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 ̊A resolution. Nature 318:618-244
    • (1985) Nature , vol.318 , pp. 618-244
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 21
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 °a reveals the molecular basis of anion selectivity
    • Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R. 2002. X-ray structure of a ClC chloride channel at 3.0 °A reveals the molecular basis of anion selectivity. Nature 415:287-944
    • (2002) Nature , vol.415 , pp. 287-944
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 22
    • 48749106109 scopus 로고    scopus 로고
    • The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport
    • Faham S,Watanabe A, Besserer GM, Cascio D, Specht A, et al. 2008. The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport. Science 321:810-144
    • (2008) Science , vol.321 , pp. 810-144
    • Faham, S.1    Watanabe, A.2    Besserer, G.M.3    Cascio, D.4    Specht, A.5
  • 23
    • 80052080449 scopus 로고    scopus 로고
    • The structural biology of β-barrel membrane proteins: A summary of recent reports
    • Fairman JW, Noinaj N, Buchanan SK. 2011. The structural biology of β-barrel membrane proteins: A summary of recent reports. Curr. Opin. Struct. Biol. 21:523-311
    • (2011) Curr. Opin. Struct. Biol , Issue.21 , pp. 523-311
    • Fairman, J.W.1    Noinaj, N.2    Buchanan, S.K.3
  • 24
    • 69249220125 scopus 로고    scopus 로고
    • Structure of a prokaryotic virtual proton pump at 3.2 ̊A resolution
    • Fang Y, Jayaram H, Shane T, Kolmakova-Partensky L, Wu F, et al. 2009. Structure of a prokaryotic virtual proton pump at 3.2 ̊A resolution. Nature 460:1040-433
    • (2009) Nature , vol.460 , pp. 1040-1433
    • Fang, Y.1    Jayaram, H.2    Shane, T.3    Kolmakova-Partensky, L.4    Wu, F.5
  • 25
    • 33846963817 scopus 로고    scopus 로고
    • A bacterial arginine-agmatine exchange transporter involved in extreme acid resistance
    • Fang Y, Kolmakova-Partensky L, Miller C. 2007. A bacterial arginine-agmatine exchange transporter involved in extreme acid resistance. J. Biol. Chem. 282:176-822
    • (2007) J. Biol. Chem , vol.282 , pp. 176-822
    • Fang, Y.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 26
    • 78049362741 scopus 로고    scopus 로고
    • Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle
    • Feng L, Campbell EB, Hsiung Y, MacKinnon R. 2010. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330:635-411
    • (2010) Science , vol.330 , pp. 635-411
    • Feng, L.1    Campbell, E.B.2    Hsiung, Y.3    MacKinnon, R.4
  • 27
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • 1807
    • Forrest LR, Kramer R, Ziegler C. 2011. The structural basis of secondary active transport mechanisms. Biochim. Biophys. Acta 1807:167-888
    • (2011) Biochim. Biophys. Acta , pp. 167-888
    • Forrest, L.R.1    Kramer, R.2    Ziegler, C.3
  • 28
    • 9444285788 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: Tales of an amateur acidophile
    • Foster JW. 2004. Escherichia coli acid resistance: Tales of an amateur acidophile. Nat. Rev. Microbiol. 2:898-9077
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 898-9077
    • Foster, J.W.1
  • 29
    • 80052103348 scopus 로고    scopus 로고
    • Femtosecond nanocrystallography using X-ray lasers for membrane protein structure determination
    • Fromme P, Spence JC. 2011. Femtosecond nanocrystallography using X-ray lasers for membrane protein structure determination. Curr. Opin. Struct. Biol. 21:509-166
    • (2011) Curr. Opin. Struct. Biol , Issue.21 , pp. 509-166
    • Fromme, P.1    Spence, J.C.2
  • 30
    • 37249030074 scopus 로고    scopus 로고
    • Structural biology: Ion pumps made crystal clear
    • Gadsby DC. 2007. Structural biology: Ion pumps made crystal clear. Nature 450:957-599
    • (2007) Nature , vol.450 , pp. 957-599
    • Gadsby, D.C.1
  • 31
    • 67349185408 scopus 로고    scopus 로고
    • Ion channels versus ion pumps: The principal difference, in principle
    • Gadsby DC. 2009. Ion channels versus ion pumps: The principal difference, in principle. Nat. Rev. Mol. Cell Biol. 10:344-522
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 344-522
    • Gadsby, D.C.1
  • 32
    • 67649200539 scopus 로고    scopus 로고
    • Structure and mechanism of an amino acid antiporter
    • Gao X, Lu F, Zhou L, Dang S, Sun L, et al. 2009. Structure and mechanism of an amino acid antiporter. Science 324:1565-688
    • (2009) Science , vol.324 , pp. 1565-1688
    • Gao, X.1    Lu, F.2    Zhou, L.3    Dang, S.4    Sun, L.5
  • 33
    • 76749095057 scopus 로고    scopus 로고
    • Mechanism of substrate recognition and transport by an amino acid antiporter
    • Gao X, Zhou L, Jiao X, Lu F, Yan C, et al. 2010. Mechanism of substrate recognition and transport by an amino acid antiporter. Nature 463:828-322
    • (2010) Nature , vol.463 , pp. 828-322
    • Gao, X.1    Zhou, L.2    Jiao, X.3    Lu, F.4    Yan, C.5
  • 34
    • 30144445932 scopus 로고    scopus 로고
    • Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
    • Garczarek F, Gerwert K. 2006. Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy. Nature 439:109-122
    • (2006) Nature , vol.439 , pp. 109-122
    • Garczarek, F.1    Gerwert, K.2
  • 35
    • 24344507684 scopus 로고    scopus 로고
    • Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other
    • Grewer C, Balani P,Weidenfeller C, Bartusel T, Tao Z, Rauen T. 2005. Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other. Biochemistry 44:11913-233
    • (2005) Biochemistry , vol.44 , pp. 11913-11243
    • Grewer, C.1    Balani, P.2    Weidenfeller, C.3    Bartusel, T.4    Tao, Z.5    Rauen, T.6
  • 38
    • 1242340323 scopus 로고    scopus 로고
    • The ABCs of solute carriers: Physiological, pathological and therapeutic implications of human membrane transport proteins
    • Hediger MA, Romero MF, Peng JB, Rolfs A, Takanaga H, Bruford EA. 2004. The ABCs of solute carriers: Physiological, pathological and therapeutic implications of human membrane transport proteins. Pflugers Arch. 447:465-688
    • (2004) Pflugers Arch , vol.447 , pp. 465-688
    • Hediger, M.A.1    Romero, M.F.2    Peng, J.B.3    Rolfs, A.4    Takanaga, H.5    Bruford, E.A.6
  • 39
    • 80054991427 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT
    • Hu NJ, Iwata S, Cameron AD, Drew D. 2011. Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT. Nature 478:408-111
    • (2011) Nature , vol.478 , pp. 408-111
    • Hu, N.J.1    Iwata, S.2    Cameron, A.D.3    Drew, D.4
  • 40
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y, Lemieux MJ, Song J, Auer M, Wang DN. 2003. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301:616-200
    • (2003) Science , vol.301 , pp. 616-200
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 41
    • 21744436321 scopus 로고    scopus 로고
    • Structure of a Na+/H++ antiporter and insights into mechanism of action and regulation by p.H
    • Hunte C, Screpanti E, Venturi M, Rimon A, Padan E, Michel H. 2005. Structure of a Na+/H++ antiporter and insights into mechanism of action and regulation by pH. Nature 435:1197-2022
    • (2005) Nature , vol.435 , pp. 1197-2022
    • Hunte, C.1    Screpanti, E.2    Venturi, M.3    Rimon, A.4    Padan, E.5    Michel, H.6
  • 42
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O. 1966. Simple allosteric model for membrane pumps. Nature 211:969-700
    • (1966) Nature , vol.211 , pp. 969-700
    • Jardetzky, O.1
  • 44
    • 84862802974 scopus 로고    scopus 로고
    • Crystal structure of a concentrative nucleoside transporter from vibrio cholerae at 2.4 å
    • Johnson ZL, Cheong CG, Lee SY. 2012. Crystal structure of a concentrative nucleoside transporter from Vibrio cholerae at 2.4 Å . Nature 483:489-933
    • (2012) Nature , vol.483 , pp. 489-933
    • Johnson, Z.L.1    Cheong, C.G.2    Lee, S.Y.3
  • 45
    • 70349335633 scopus 로고    scopus 로고
    • ABC transporters: A riddle wrapped in a mystery inside an enigma
    • Jones PM, O'Mara ML, George AM. 2009. ABC transporters: A riddle wrapped in a mystery inside an enigma. Trends Biochem. Sci. 34:520-311
    • (2009) Trends Biochem. Sci , vol.34 , pp. 520-311
    • Jones, P.M.1    O'Mara, M.L.2    George, A.M.3
  • 47
    • 84859568204 scopus 로고    scopus 로고
    • Membrane pores in the pathogenesis of neurodegenerative disease
    • Kagan BL. 2012. Membrane pores in the pathogenesis of neurodegenerative disease. Prog. Mol. Biol. Transl. Sci. 107:295-3255
    • (2012) Prog. Mol. Biol. Transl. Sci , Issue.107 , pp. 295-3255
    • Kagan, B.L.1
  • 49
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • Krishnamurthy H, Gouaux E. 2012. X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481:469-744
    • (2012) Nature , vol.481 , pp. 469-744
    • Krishnamurthy, H.1    Gouaux, E.2
  • 50
    • 66249098083 scopus 로고    scopus 로고
    • Unlocking the molecular secrets of sodium-coupled transporters
    • Krishnamurthy H, Piscitelli CL, Gouaux E. 2009. Unlocking the molecular secrets of sodium-coupled transporters. Nature 459:347-555
    • (2009) Nature , vol.459 , pp. 347-555
    • Krishnamurthy, H.1    Piscitelli, C.L.2    Gouaux, E.3
  • 51
    • 49749153798 scopus 로고    scopus 로고
    • The role of TrmB and TrmB-like transcriptional regulators for sugar transport and metabolism in the hyperthermophilic archaeon Pyrococcus furiosus
    • Lee SJ, Surma M, Hausner W, Thomm M, Boos W. 2008. The role of TrmB and TrmB-like transcriptional regulators for sugar transport and metabolism in the hyperthermophilic archaeon Pyrococcus furiosus. Arch. Microbiol. 190:247-566
    • (2008) Arch. Microbiol , vol.190 , pp. 247-566
    • Lee, S.J.1    Surma, M.2    Hausner, W.3    Thomm, M.4    Boos, W.5
  • 52
    • 72049114961 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the kidney urea transporter
    • Levin EJ, Quick M, Zhou M. 2009. Crystal structure of a bacterial homologue of the kidney urea transporter. Nature 462:757-611
    • (2009) Nature , vol.462 , pp. 757-611
    • Levin, E.J.1    Quick, M.2    Zhou, M.3
  • 53
    • 84863012221 scopus 로고    scopus 로고
    • Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger
    • Liao J, Li H, Zeng W, Sauer DB, Belmares R, Jiang Y. 2012. Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger. Science 335:686-900
    • (2012) Science , vol.335 , pp. 686-900
    • Liao, J.1    Li, H.2    Zeng, W.3    Sauer, D.B.4    Belmares, R.5    Jiang, Y.6
  • 54
    • 84861421976 scopus 로고    scopus 로고
    • Structures from anomalous diffraction of native biological macromolecules
    • Liu Q, Dahmane T, Zhang Z, Assur Z, Brasch J, et al. 2012. Structures from anomalous diffraction of native biological macromolecules. Science 336:1033-377
    • (2012) Science , vol.336 , pp. 1033-1377
    • Liu, Q.1    Dahmane, T.2    Zhang, Z.3    Assur, Z.4    Brasch, J.5
  • 55
    • 78651100936 scopus 로고    scopus 로고
    • Multi-crystal anomalous diffraction for low-resolution macromolecular phasing
    • Liu Q, Zhang Z, Hendrickson WA. 2011. Multi-crystal anomalous diffraction for low-resolution macromolecular phasing. Acta Crystallogr. D 67:45-599
    • (2011) Acta Crystallogr , vol.D67 , pp. 45-599
    • Liu, Q.1    Zhang, Z.2    Hendrickson, W.A.3
  • 56
    • 61449341855 scopus 로고    scopus 로고
    • Review Structure and mechanism of ATP-binding cassette transporters
    • Locher KP. 2009. Review. Structure and mechanism of ATP-binding cassette transporters. Philos. Trans. R. Soc. Lond. B Biol. Sci. 364:239-455
    • (2009) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.364 , pp. 239-455
    • Locher, K.P.1
  • 57
    • 0037052565 scopus 로고    scopus 로고
    • The e coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher KP, Lee AT, Rees DC. 2002. The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism. Science 296:1091-988
    • (2002) Science , vol.296 , pp. 1091-1988
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 58
    • 79954573127 scopus 로고    scopus 로고
    • Structure and mechanism of the uracil transporter UraA
    • Lu F, Li S, Jiang Y, Jiang J, Fan H, et al. 2011. Structure and mechanism of the uracil transporter UraA. Nature 472:243-466
    • (2011) Nature , vol.472 , pp. 243-466
    • Lu, F.1    Li, S.2    Jiang, Y.3    Jiang, J.4    Fan, H.5
  • 59
    • 84862819559 scopus 로고    scopus 로고
    • Structure and mechanism of a glutamate-GABA antiporter
    • Ma D, Lu P, Yan C, Fan C, Yin P, et al. 2012. Structure and mechanism of a glutamate-GABA antiporter. Nature 483:632-366
    • (2012) Nature , vol.483 , pp. 632-366
    • Ma, D.1    Lu, P.2    Yan, C.3    Fan, C.4    Yin, P.5
  • 60
    • 84856297467 scopus 로고    scopus 로고
    • Crystal structure of the human two-pore domain potassium channel K2P1
    • Miller AN, Long SB. 2012. Crystal structure of the human two-pore domain potassium channel K2P1. Science 335:432-366
    • (2012) Science , vol.335 , pp. 432-366
    • Miller, A.N.1    Long, S.B.2
  • 61
    • 33645296826 scopus 로고    scopus 로고
    • ClC chloride channels viewed through a transporter lens
    • Miller C. 2006. ClC chloride channels viewed through a transporter lens. Nature 440:484-899
    • (2006) Nature , vol.440 , pp. 484-899
    • Miller, C.1
  • 62
    • 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. 25:1177-833
    • (2006) EMBO J. , vol.25 , pp. 1177-1833
    • Mirza, O.1    Guan, L.2    Verner, G.3    Iwata, S.4    Kaback, H.R.5
  • 64
    • 78751604619 scopus 로고    scopus 로고
    • Crystal structure of a prokaryotic homologue of themammalian oligopeptide-proton symporters, PepT1 and PepT2
    • Newstead S, Drew D, Cameron AD, Postis VL, Xia X, et al. 2011. Crystal structure of a prokaryotic homologue of themammalian oligopeptide-proton symporters, PepT1 and PepT2. EMBO J. 30:417-266
    • (2011) EMBO J. , Issue.30 , pp. 417-266
    • Newstead, S.1    Drew, D.2    Cameron, A.D.3    Postis, V.L.4    Xia, X.5
  • 68
    • 65249169367 scopus 로고    scopus 로고
    • Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation
    • Quick M, Winther AM, Shi L, Nissen P, Weinstein H, Javitch JA. 2009. Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation. Proc. Natl. Acad. Sci. USA 106:5563-688
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5563-5688
    • Quick, M.1    Winther, A.M.2    Shi, L.3    Nissen, P.4    Weinstein, H.5    Javitch, J.A.6
  • 70
    • 0027233420 scopus 로고
    • TheMIP family of integral membrane channel proteins: Sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins
    • Reizer J, Reizer A, SaierMHJr. 1993. TheMIP family of integral membrane channel proteins: Sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins. Crit. Rev. Biochem. Mol. Biol. 28:235-577
    • (1993) Crit. Rev. Biochem. Mol. Biol , vol.28 , pp. 235-577
    • Reizer, J.1    Reizer, A.2    Saier Jr., M.H.3
  • 71
    • 34250883333 scopus 로고    scopus 로고
    • Large-scale comparative genomic analyses of cytoplasmicmembrane transport systems in prokaryotes
    • RenQ, Paulsen IT. 2007. Large-scale comparative genomic analyses of cytoplasmicmembrane transport systems in prokaryotes. J. Mol. Microbiol. Biotechnol. 12:165-799
    • (2007) J. Mol. Microbiol. Biotechnol , vol.12 , pp. 165-799
    • Renq Paulsen, I.T.1
  • 73
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • Reyes N, Ginter C, Boudker O. 2009. Transport mechanism of a bacterial homologue of glutamate transporters. Nature 462:880-855
    • (2009) Nature , vol.462 , pp. 880-855
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 74
    • 36448978229 scopus 로고    scopus 로고
    • GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function
    • Rosenbaum DM, Cherezov V, Hanson MA, Rasmussen SG, Thian FS, et al. 2007. GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function. Science 318:1266-733
    • (2007) Science , vol.318 , pp. 1266-1733
    • Rosenbaum, D.M.1    Cherezov, V.2    Hanson, M.A.3    Rasmussen, S.G.4    Thian, F.S.5
  • 75
    • 0034718616 scopus 로고    scopus 로고
    • Unraveling the mechanism of the lactose permease of Escherichia coli
    • Sahin-Toth M, Karlin A, Kaback HR. 2000. Unraveling the mechanism of the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. USA 97:10729-322
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10729-10332
    • Sahin-Toth, M.1    Karlin, A.2    Kaback, H.R.3
  • 77
    • 67649867931 scopus 로고    scopus 로고
    • A gating model for the archeal voltage-dependent K++channel KvAP in DPhPC and POPE:POPG decane lipid bilayers
    • Schmidt D, Cross SR, MacKinnon R. 2009. A gating model for the archeal voltage-dependent K++channel KvAP in DPhPC and POPE:POPG decane lipid bilayers. J. Mol. Biol. 390:902-122
    • (2009) J. Mol. Biol , vol.390 , pp. 902-122
    • Schmidt, D.1    Cross, S.R.2    MacKinnon, R.3
  • 78
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • Schmidt D, Jiang QX, MacKinnon R. 2006. Phospholipids and the origin of cationic gating charges in voltage sensors. Nature 444:775-799
    • (2006) Nature , vol.444 , pp. 775-799
    • Schmidt, D.1    Jiang, Q.X.2    MacKinnon, R.3
  • 80
    • 34447637751 scopus 로고    scopus 로고
    • Discontinuous membrane helices in transport proteins and their correlation with function
    • Screpanti E,Hunte C. 2007. Discontinuous membrane helices in transport proteins and their correlation with function. J. Struct. Biol. 159:261-677
    • (2007) J. Struct. Biol , vol.159 , pp. 261-677
    • Screpanti, E.1    Hunte, C.2
  • 81
    • 79551667263 scopus 로고    scopus 로고
    • Single mimivirus particles intercepted and imaged with an X-ray laser
    • Seibert MM, Ekeberg T, Maia FR, Svenda M, Andreasson J, et al. 2011. Single mimivirus particles intercepted and imaged with an X-ray laser. Nature 470:78-811
    • (2011) Nature , vol.470 , pp. 78-811
    • Seibert, M.M.1    Ekeberg, T.2    Maia, F.R.3    Svenda, M.4    Andreasson, J.5
  • 82
    • 69249116947 scopus 로고    scopus 로고
    • Structure and mechanism of a Na+-independent amino acid transporter
    • Shaffer PL, Goehring A, Shankaranarayanan A, Gouaux E. 2009. Structure and mechanism of a Na+-independent amino acid transporter. Science 325:1010-144
    • (2009) Science , vol.325 , pp. 1010-1144
    • Shaffer, P.L.1    Goehring, A.2    Shankaranarayanan, A.3    Gouaux, E.4
  • 83
    • 50049095291 scopus 로고    scopus 로고
    • The dynamics of the MBP-MalFGK2 interaction: A prototype for binding protein dependent ABC-transporter systems
    • Shilton BH. 2008. The dynamics of the MBP-MalFGK2 interaction: A prototype for binding protein dependent ABC-transporter systems. Biochim. Biophys. Acta 1778:1772-800
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1772-1800
    • Shilton, B.H.1
  • 84
    • 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 NG, Hadden JM, et al. 2011. Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1.Science 328:470-733
    • (2011) Science , vol.328 , pp. 470-733
    • Shimamura, T.1    Weyand, S.2    Beckstein, O.3    Rutherford, N.G.4    Hadden, J.M.5
  • 85
    • 58149233796 scopus 로고    scopus 로고
    • A competitive inhibitor traps LeuT in an open-to-out conformation
    • Singh SK, Piscitelli CL, Yamashita A, Gouaux E. 2008. A competitive inhibitor traps LeuT in an open-to-out conformation. Science 322:1655-611
    • (2008) Science , vol.322 , pp. 1655-1621
    • Singh, S.K.1    Piscitelli, C.L.2    Yamashita, A.3    Gouaux, E.4
  • 86
    • 34548178234 scopus 로고    scopus 로고
    • Antidepressant binding site in a bacterial homologue of neurotransmitter transporters
    • Singh SK, Yamashita A, Gouaux E. 2007. Antidepressant binding site in a bacterial homologue of neurotransmitter transporters. Nature 448:952-566
    • (2007) Nature , vol.448 , pp. 952-566
    • Singh, S.K.1    Yamashita, A.2    Gouaux, E.3
  • 87
    • 0025472294 scopus 로고
    • The fourth Datta lecture the energy coupled exchange of Na+ for K+ across the cell membrane. The Na+, K+-pump
    • Skou JC. 1990. The fourth Datta lecture. The energy coupled exchange of Na+ for K+ across the cell membrane. The Na+, K+-pump. FEBS Lett. 268:314-244
    • (1990) FEBS Lett , vol.268 , pp. 314-244
    • Skou, J.C.1
  • 89
    • 84865237281 scopus 로고    scopus 로고
    • Alternating access mechanism in the POT family of oligopeptide transporters
    • Solcan N, Kwok J, Fowler PW, Cameron AD, Drew D, et al. 2012. Alternating access mechanism in the POT family of oligopeptide transporters. EMBO J. 31:3411-211
    • (2012) EMBO J. , Issue.31 , pp. 3411-3221
    • Solcan, N.1    Kwok, J.2    Fowler, P.W.3    Cameron, A.D.4    Drew, D.5
  • 90
    • 84866277256 scopus 로고    scopus 로고
    • Dynamics of the L-fucose/H+ symporter revealed by fluorescence spectroscopy
    • Sugihara J, Sun L, Yan N, Kaback HR. 2012. Dynamics of the L-fucose/H+ symporter revealed by fluorescence spectroscopy. Proc. Natl. Acad. Sci. USA 109:14847-511
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 14847-14521
    • Sugihara, J.1    Sun, L.2    Yan, N.3    Kaback, H.R.4
  • 91
    • 84867657593 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of glucose transporters GLUT1-4
    • Sun L, Zeng X, Yan C, Sun X, Gong X, et al. 2012. Crystal structure of a bacterial homologue of glucose transporters GLUT1-4. Nature 490:361-666
    • (2012) Nature , vol.490 , pp. 361-666
    • Sun, L.1    Zeng, X.2    Yan, C.3    Sun, X.4    Gong, X.5
  • 92
    • 77950476282 scopus 로고    scopus 로고
    • Crystal structure of the carnitine transporter and insights into the antiport mechanism
    • Tang L, Bai L, Wang WH, Jiang T. 2010. Crystal structure of the carnitine transporter and insights into the antiport mechanism. Nat. Struct. Mol. Biol. 17:492-966
    • (2010) Nat. Struct. Mol. Biol , Issue.17 , pp. 492-966
    • Tang, L.1    Bai, L.2    Wang, W.H.3    Jiang, T.4
  • 93
    • 82955168417 scopus 로고    scopus 로고
    • First crystal structures of Na+,K+-ATPase: New light on the oldest ion pump
    • Toyoshima C, Kanai R, Cornelius F. 2012. First crystal structures of Na+,K+-ATPase: New light on the oldest ion pump. Structure 19:1732-388
    • (2012) Structure , vol.19 , pp. 1732-1398
    • Toyoshima, C.1    Kanai, R.2    Cornelius, F.3
  • 94
    • 84857992685 scopus 로고    scopus 로고
    • Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog
    • Verdon G, Boudker O. 2012. Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog. Nat. Struct. Mol. Biol. 19:355-577
    • (2012) Nat. Struct. Mol. Biol , Issue.19 , pp. 355-577
    • Verdon, G.1    Boudker, O.2
  • 96
    • 77449091710 scopus 로고    scopus 로고
    • Structure and mechanism of a pentameric formate channel
    • Waight AB, Love J,Wang DN. 2010. Structure and mechanism of a pentameric formate channel. Nat. Struct. Mol. Biol. 17:31-377
    • (2010) Nat. Struct. Mol. Biol , Issue.17 , pp. 31-377
    • Waight, A.B.1    Love, J.2    Wang, D.N.3
  • 97
    • 84862790971 scopus 로고    scopus 로고
    • Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context
    • Wang H, Elferich J, Gouaux E. 2012. Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context. Nat. Struct. Mol. Biol. 19:212-199
    • (2012) Nat. Struct. Mol. Biol , Issue.19 , pp. 212-199
    • Wang, H.1    Elferich, J.2    Gouaux, E.3
  • 98
    • 70849106457 scopus 로고    scopus 로고
    • Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel
    • Wang Y, Huang Y, Wang J, Cheng C, Huang W, et al. 2009. Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel. Nature 462:467-722
    • (2009) Nature , vol.462 , pp. 467-722
    • Wang, Y.1    Huang, Y.2    Wang, J.3    Cheng, C.4    Huang, W.5
  • 99
    • 78650306568 scopus 로고    scopus 로고
    • The mechanism of sodium and substrate release from the binding pocket of vSGLT
    • Watanabe A, Choe S, Chaptal V, Rosenberg JM, Wright EM, et al. 2010. The mechanism of sodium and substrate release from the binding pocket of vSGLT. Nature 468:988-911
    • (2010) Nature , vol.468 , pp. 988-911
    • Watanabe, A.1    Choe, S.2    Chaptal, V.3    Rosenberg, J.M.4    Wright, E.M.5
  • 100
    • 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, Mirza O, et al. 2008. Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter. Science 322:709-133
    • (2008) Science , vol.322 , pp. 709-133
    • Weyand, S.1    Shimamura, T.2    Yajima, S.3    Suzuki, S.4    Mirza, O.5
  • 101
    • 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
    • Widdas WF. 1952. Inability of diffusion to account for placental glucose transfer in the sheep and consideration of the kinetics of a possible carrier transfer. J. Physiol. 118:23-399
    • (1952) J. Physiol , vol.118 , pp. 23-399
    • Widdas, W.F.1
  • 102
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters
    • Yamashita A, Singh SK, Kawate T, Jin Y, Gouaux E. 2005. Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters. Nature 437:215-233
    • (2005) Nature , vol.437 , pp. 215-233
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 103
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool D, Boudker O, Jin Y, Gouaux E. 2004. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431:811-188
    • (2004) Nature , vol.431 , pp. 811-188
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 104
    • 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 312:741-444
    • (2006) Science , vol.312 , pp. 741-444
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 105
    • 77952402284 scopus 로고    scopus 로고
    • Single-molecule dynamics of gating in a neurotransmitter transporter homologue
    • Zhao Y, Terry D, Shi L, Weinstein H, Blanchard SC, Javitch JA. 2010. Single-molecule dynamics of gating in a neurotransmitter transporter homologue. Nature 465:188-933
    • (2010) Nature , vol.465 , pp. 188-933
    • Zhao, Y.1    Terry, D.2    Shi, L.3    Weinstein, H.4    Blanchard, S.C.5    Javitch, J.A.6
  • 106
    • 34548684744 scopus 로고    scopus 로고
    • LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake
    • Zhou Z, Zhen J, Karpowich NK, Goetz RM, Law CJ, et al. 2007. LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake. Science 317:1390-933
    • (2007) Science , vol.317 , pp. 1390-1933
    • Zhou, Z.1    Zhen, J.2    Karpowich, N.K.3    Goetz, R.M.4    Law, C.J.5


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