메뉴 건너뛰기




Volumn 65, Issue 2, 2007, Pages 250-257

Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE;

EID: 34447311648     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05792.x     Document Type: Short Survey
Times cited : (133)

References (47)
  • 1
    • 31944431842 scopus 로고    scopus 로고
    • ABC transporter architecture and regulatory roles of accessory domains
    • Biemans-Oldehinkel, E., Doeven, M.K. Poolman, B. (2006) ABC transporter architecture and regulatory roles of accessory domains. FEBS Lett 580 : 1023 1035.
    • (2006) FEBS Lett , vol.580 , pp. 1023-1035
    • Biemans-Oldehinkel, E.1    Doeven, M.K.2    Poolman, B.3
  • 2
    • 0037168666 scopus 로고    scopus 로고
    • The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter
    • Borths, E.L., Locher, K.P., Lee, A.T. Rees, D.C. (2002) The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proc Natl Acad Sci USA 99 : 16642 16647.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16642-16647
    • Borths, E.L.1    Locher, K.P.2    Lee, A.T.3    Rees, D.C.4
  • 3
  • 5
    • 0030043695 scopus 로고    scopus 로고
    • A functionally defective allele of TAP1 results in loss of MHC class I antigen presentation in a human lung cancer
    • Chen, H.L., Gabrilovich, D., Tampe, R., Girgis, K.R., Nadaf, S. Carbone, D.P. (1996) A functionally defective allele of TAP1 results in loss of MHC class I antigen presentation in a human lung cancer. Nat Genet 13 : 210 213.
    • (1996) Nat Genet , vol.13 , pp. 210-213
    • Chen, H.L.1    Gabrilovich, D.2    Tampe, R.3    Girgis, K.R.4    Nadaf, S.5    Carbone, D.P.6
  • 6
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen, J., Sharma, S., Quiocho, F.A. Davidson, A.L. (2001) Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport. Proc Natl Acad Sci USA 98 : 1525 1530.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 7
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen, J., Lu, G., Lin, J., Davidson, A.L. Quiocho, F.A. (2003) A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol Cell 12 : 651 661.
    • (2003) Mol Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 8
    • 0027396907 scopus 로고
    • Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli
    • Dassa, E. Muir, S. (1993) Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol Microbiol 7 : 29 38.
    • (1993) Mol Microbiol , vol.7 , pp. 29-38
    • Dassa, E.1    Muir, S.2
  • 9
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A.L. Chen, J. (2004) ATP-binding cassette transporters in bacteria. Annu Rev Biochem 73 : 241 268.
    • (2004) Annu Rev Biochem , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 10
    • 0029868327 scopus 로고    scopus 로고
    • The maltose transport system of Escherichia coli displays positive cooperativity in ATP hydrolysis
    • Davidson, A.L., Laghaeian, S.S. Mannering, D.E. (1996) The maltose transport system of Escherichia coli displays positive cooperativity in ATP hydrolysis. J Biol Chem 271 : 4858 4863.
    • (1996) J Biol Chem , vol.271 , pp. 4858-4863
    • Davidson, A.L.1    Laghaeian, S.S.2    Mannering, D.E.3
  • 11
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R.J.P. Locher, K.P. (2006) Structure of a bacterial multidrug ABC transporter. Nature 443 : 180 185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 12
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson, R.J.P. Locher, K.P. (2007) Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett 581 : 935 938.
    • (2007) FEBS Lett , vol.581 , pp. 935-938
    • Dawson, R.J.P.1    Locher, K.P.2
  • 14
    • 0036774002 scopus 로고    scopus 로고
    • ABC transporters: One, two or four extracytoplasmic substrate-binding sites?
    • van der Heide, T. Poolman, B. (2002) ABC transporters: one, two or four extracytoplasmic substrate-binding sites? EMBO Rep 3 : 938 943.
    • (2002) EMBO Rep , vol.3 , pp. 938-943
    • Van Der Heide, T.1    Poolman, B.2
  • 15
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins, C.F. Linton, K.J. (2004) The ATP switch model for ABC transporters. Nat Struct Mol Biol 11 : 918 926.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 17
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein, K., Frei, D.C. Locher, K.P. (2007) Structure of an ABC transporter in complex with its binding protein. Nature 446 : 213 216.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 18
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K.P., Karcher, A., Shin, D.S., Craig, L., Arthur, L.M., Carney, J.P. Tainer, J.A. (2000) Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101 : 789 800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 19
    • 0032479280 scopus 로고    scopus 로고
    • Mechanism of action of human P-glycoprotein ATPase activity - Photochemical cleavage during a catalytic transition state using orthovanadate reveals cross-talk between the two ATP sites
    • Hrycyna, C.A., Ramachandra, M., Ambudkar, S.V., Ko, Y.H., Pedersen, P.L., Pastan, I. Gottesman, M.M. (1998) Mechanism of action of human P-glycoprotein ATPase activity - photochemical cleavage during a catalytic transition state using orthovanadate reveals cross-talk between the two ATP sites. J Biol Chem 273 : 16631 16634.
    • (1998) J Biol Chem , vol.273 , pp. 16631-16634
    • Hrycyna, C.A.1    Ramachandra, M.2    Ambudkar, S.V.3    Ko, Y.H.4    Pedersen, P.L.5    Pastan, I.6    Gottesman, M.M.7
  • 20
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L.W., Wang, I.X.Y., Nikaido, K., Liu, P.Q., Ames, G.F.L. Kim, S.H. (1998) Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396 : 703 707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.Y.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.L.5    Kim, S.H.6
  • 21
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. (1966) Simple allosteric model for membrane pumps. Nature 211 : 969 970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 22
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • Jones, P.M. George, A.M. (1999) Subunit interactions in ABC transporters: towards a functional architecture. FEMS Microbiol Lett 179 : 187 202.
    • (1999) FEMS Microbiol Lett , vol.179 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 23
    • 1842610700 scopus 로고    scopus 로고
    • The ABC transporter structure and mechanism: Perspectives on recent research
    • Jones, P.M. George, A.M. (2004) The ABC transporter structure and mechanism: perspectives on recent research. Cell Mol Life Sci 61 : 682 699.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 682-699
    • Jones, P.M.1    George, A.M.2
  • 24
    • 1642290656 scopus 로고    scopus 로고
    • Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP)
    • Koch, J., Guntrum, R., Heintke, S., Kyritsis, C. Tampe, R. (2004) Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP). J Biol Chem 279 : 10142 10147.
    • (2004) J Biol Chem , vol.279 , pp. 10142-10147
    • Koch, J.1    Guntrum, R.2    Heintke, S.3    Kyritsis, C.4    Tampe, R.5
  • 25
    • 4544231184 scopus 로고    scopus 로고
    • Glycerol-3-phosphate transporter of Escherichia coli: Structure, function and regulation
    • Lemieux, M.J., Huang, Y. Wang, D.-N. (2004) Glycerol-3-phosphate transporter of Escherichia coli: structure, function and regulation. Res Microbiol 155 : 623 629.
    • (2004) Res Microbiol , vol.155 , pp. 623-629
    • Lemieux, M.J.1    Huang, Y.2    Wang, D.-N.3
  • 26
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K.P., Lee, A.T. Rees, D.C. (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296 : 1091 1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 27
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M., Hofnung, N. Dassa, E. (1997) Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J 16 : 3066 3077.
    • (1997) EMBO J , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, N.2    Dassa, E.3
  • 28
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • Patzlaff, J.S., van der Heide, T. Poolman, B. (2003) The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA. J Biol Chem 278 : 29546 29551.
    • (2003) J Biol Chem , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    Van Der Heide, T.2    Poolman, B.3
  • 29
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • Pinkett, H.W., Lee, A.T., Lum, P., Locher, K.P. Rees, D.C. (2007) An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315 : 373 377.
    • (2007) Science , vol.315 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 30
    • 13444266621 scopus 로고    scopus 로고
    • P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: A combined photoaffinity labeling-protein homology modeling approach
    • Pleban, K., Kopp, S., Csaszar, E., Peer, M., Hrebicek, T., Rizzi, A., et al. (2005) P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: a combined photoaffinity labeling-protein homology modeling approach. Mol Pharmacol 67 : 365 374.
    • (2005) Mol Pharmacol , vol.67 , pp. 365-374
    • Pleban, K.1    Kopp, S.2    Csaszar, E.3    Peer, M.4    Hrebicek, T.5    Rizzi, A.6
  • 31
    • 29144466584 scopus 로고    scopus 로고
    • Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I
    • Procko, E., Raghuraman, G., Wiley, D.C., Raghavan, M. Gaudet, R. (2005) Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I. Immunol Cell Biol 83 : 475 482.
    • (2005) Immunol Cell Biol , vol.83 , pp. 475-482
    • Procko, E.1    Raghuraman, G.2    Wiley, D.C.3    Raghavan, M.4    Gaudet, R.5
  • 32
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F.A. Ledvina, P.S. (1996) Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol Microbiol 20 : 17 25.
    • (1996) Mol Microbiol , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 33
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • Ramachandra, M., Ambudkar, S.V., Chen, D., Hrycyna, C.A., Dey, S., Gottesman, M.M. Pastan, I. (1998) Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state. Biochemistry 37 : 5010 5019.
    • (1998) Biochemistry , vol.37 , pp. 5010-5019
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6    Pastan, I.7
  • 34
    • 17944370228 scopus 로고    scopus 로고
    • Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle
    • Rosenberg, M.F., Velarde, G., Ford, R.C., Martin, C., Berridge, G., Kerr, I.D., et al. (2001) Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle. EMBO J 20 : 5615 5625.
    • (2001) EMBO J , vol.20 , pp. 5615-5625
    • Rosenberg, M.F.1    Velarde, G.2    Ford, R.C.3    Martin, C.4    Berridge, G.5    Kerr, I.D.6
  • 35
    • 0034646468 scopus 로고    scopus 로고
    • Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein
    • Sauna, Z.E. Ambudkar, S.V. (2000) Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein. Proc Natl Acad Sci USA 97 : 2515 2520.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2515-2520
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 36
    • 0035933843 scopus 로고    scopus 로고
    • Distinct functions of the ATP binding cassettes of transporters associated with antigen processing - A mutational analysis of Walker a and B sequences
    • Saveanu, L., Daniel, S. van Endert, P.M. (2001) Distinct functions of the ATP binding cassettes of transporters associated with antigen processing - a mutational analysis of Walker A and B sequences. J Biol Chem 276 : 22107 22113.
    • (2001) J Biol Chem , vol.276 , pp. 22107-22113
    • Saveanu, L.1    Daniel, S.2    Van Endert, P.M.3
  • 37
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • Schneider, E. Hunke, S. (1998) ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains. FEMS Microbiol Rev 22 : 1 20.
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 39
    • 0032548468 scopus 로고    scopus 로고
    • P-glycoprotein shows strong catalytic cooperativity between the two nucleotide sites
    • Senior, A.E. Bhagat, S. (1998) P-glycoprotein shows strong catalytic cooperativity between the two nucleotide sites. Biochemistry 37 : 831 836.
    • (1998) Biochemistry , vol.37 , pp. 831-836
    • Senior, A.E.1    Bhagat, S.2
  • 40
    • 0030782511 scopus 로고    scopus 로고
    • Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities
    • Shapiro, A.B. Ling, V. (1997) Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities. Eur J Biochem 250 : 130 137.
    • (1997) Eur J Biochem , vol.250 , pp. 130-137
    • Shapiro, A.B.1    Ling, V.2
  • 41
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P.C., Karpowich, N., Millen, L., Moody, J.E., Rosen, J., Thomas, P.J. Hunt, J.F. (2002) ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10 : 139 149.
    • (2002) Mol Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 42
    • 0642272487 scopus 로고    scopus 로고
    • An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulphide cross-linking and homology modeling
    • Stenham, D.R., Campbell, J.D., Sansom, M.S.P., Higgins, C.F., Kerr, I.D. Linton, K.J. (2003) An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulphide cross-linking and homology modeling. FASEB J 17 : 2287 2289.
    • (2003) FASEB J , vol.17 , pp. 2287-2289
    • Stenham, D.R.1    Campbell, J.D.2    Sansom, M.S.P.3    Higgins, C.F.4    Kerr, I.D.5    Linton, K.J.6
  • 43
    • 0026641782 scopus 로고
    • The spectrum of cystic-fibrosis mutations
    • Tsui, L.C. (1992) The spectrum of cystic-fibrosis mutations. Trends Genet 8 : 392 398.
    • (1992) Trends Genet , vol.8 , pp. 392-398
    • Tsui, L.C.1
  • 44
    • 0034212332 scopus 로고    scopus 로고
    • The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
    • van Veen, H.W., Margolles, A., Muller, M., Higgins, C.F. Konings, W.N. (2000) The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism. EMBO J 19 : 2503 2514.
    • (2000) EMBO J , vol.19 , pp. 2503-2514
    • Van Veen, H.W.1    Margolles, A.2    Muller, M.3    Higgins, C.F.4    Konings, W.N.5
  • 45
    • 0037163877 scopus 로고    scopus 로고
    • A new experimental approach to detect long-range conformational changes transmitted between the membrane and cytosolic domains of LmrA, a bacterial multidrug transporter
    • Vigano, C., Grimard, V., Margolles, A., Goormaghtigh, E., Van Veen, H.W., Konings, W.N. Ruysschaert, J.M. (2002) A new experimental approach to detect long-range conformational changes transmitted between the membrane and cytosolic domains of LmrA, a bacterial multidrug transporter. FEBS Lett 530 : 197 203.
    • (2002) FEBS Lett , vol.530 , pp. 197-203
    • Vigano, C.1    Grimard, V.2    Margolles, A.3    Goormaghtigh, E.4    Van Veen, H.W.5    Konings, W.N.6    Ruysschaert, J.M.7
  • 46
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva, J., Jenewein, S., Jumpertz, T., Holland, I.B. Schmitt, L. (2005) H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J 24 : 1901 1910.
    • (2005) EMBO J , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 47
    • 0037666795 scopus 로고    scopus 로고
    • Evidence for two interacting ligand binding sites in human multidrug resistance protein 2 (ATP binding cassette C2)
    • Zelcer, N., Huisman, M.T., Reid, G., Wieling, P., Breedveld, P., Kuil, A., et al. (2003) Evidence for two interacting ligand binding sites in human multidrug resistance protein 2 (ATP binding cassette C2). J Biol Chem 278 : 23538 23544.
    • (2003) J Biol Chem , vol.278 , pp. 23538-23544
    • Zelcer, N.1    Huisman, M.T.2    Reid, G.3    Wieling, P.4    Breedveld, P.5    Kuil, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.