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Volumn 14, Issue 4, 2004, Pages 426-431

Structure and mechanism of ABC transporters

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; BINDING PROTEIN; CYANOCOBALAMIN; EDETIC ACID; MULTIDRUG RESISTANCE PROTEIN 1; PROTEIN BTUCD; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG;

EID: 4143115811     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.06.005     Document Type: Review
Times cited : (149)

References (40)
  • 1
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • E. Schneider, and S. Hunke ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains FEMS Microbiol Rev 22 1998 1 20
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 1-20
    • Schneider1    Hunke, S.E.2
  • 2
    • 0032951188 scopus 로고    scopus 로고
    • Getting in or out: Early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters
    • W. Saurin, M. Hofnung, and E. Dassa Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters J Mol Evol 48 1999 22 41
    • (1999) J Mol Evol , vol.48 , pp. 22-41
    • Saurin, W.1    Hofnung2    Dassa, E.M.3
  • 3
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules organisms from bacteria to humans
    • I.B. Holland, and M.A. Blight ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules organisms from bacteria to humans J Mol Biol 293 1999 381 399
    • (1999) J Mol Biol , vol.293 , pp. 381-399
    • Holland1    Blight, M.A.I.B.2
  • 4
    • 0035685449 scopus 로고    scopus 로고
    • Complete characterization of the human ABC gene family
    • M. Dean, and R. Allikmets Complete characterization of the human ABC gene family J Bioenerg Biomembr 33 2001 475 479
    • (2001) J Bioenerg Biomembr , vol.33 , pp. 475-479
    • Dean1    Allikmets, R.M.2
  • 5
    • 0032323640 scopus 로고    scopus 로고
    • Overview of bacterial ABC transporters
    • H. Nikaido, and J.A. Hall Overview of bacterial ABC transporters Methods Enzymol 292 1998 3 20
    • (1998) Methods Enzymol , vol.292 , pp. 3-20
    • Nikaido1    Hall, J.A.H.2
  • 6
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • G. Chang, and C.B. Roth Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters Science 293 2001 1793 1800
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang1    Roth, C.B.G.2
  • 7
    • 0038799725 scopus 로고    scopus 로고
    • Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation
    • G. Chang Structure of MsbA from Vibrio cholera: a multidrug resistance ABC transporter homolog in a closed conformation J Mol Biol 330 2003 419 430 The author presents the 3.8 Å resolution crystal structure of the lipid A flippase MsbA from a different organism and in a different conformation to that reported earlier [6]. The structure is more compact than the previous one, and the ABC domains are arranged with their signature motifs facing the symmetry axis and contacting the opposing monomer. The structure of the ABC domain is distinct from those of all other ABC domains solved to date because the β-subdomain (including the P-loops) is rotated away from the α-helical subdomain by 120°.
    • (2003) J Mol Biol , vol.330 , pp. 419-430
    • Chang, G.1
  • 8
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • K.P. Locher, A.T. Lee, and D.C. Rees The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism Science 296 2002 1091 1098 The authors present the BtuCD crystal structure at 3.2 Å resolution.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee2    Rees, D.C.A.T.3
  • 9
    • 0037168666 scopus 로고    scopus 로고
    • The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter
    • E.L. Borths, K.P. Locher, A.T. Lee, and D.C. Rees The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter Proc Natl Acad Sci USA 99 2002 16642 16647 The authors reveal the crystal structure of the E. coli B12-binding protein BtuF and demonstrate an in vitro complex between BtuF and BtuCD.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16642-16647
    • Borths, E.L.1    Locher, K.P.2    Lee3    Rees, D.C.A.T.4
  • 10
    • 0037424465 scopus 로고    scopus 로고
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding J Biol Chem 278 2003 8429 8434 The crystal structure of E. coli BtuF, free and with bound B12, reveals the conformational changes upon B12 binding.
    • (2003) J Biol Chem , vol.278 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith3    Hunt, J.F.P.C.4
  • 11
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • L.W. Hung, I.X.Y. Wang, K. Nikaido, P.Q. Liu, G.F.L. Ames, and S.H. Kim Crystal structure of the ATP-binding subunit of an ABC transporter Nature 396 1998 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    Ames5    Kim, S.H.G.F.L.6
  • 12
    • 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
    • K.P. Hopfner, A. Karcher, D.S. Shin, L. Craig, L.M. Arthur, J.P. Carney, and J.A. Tainer Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily Cell 101 2000 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    Carney6    Tainer, J.A.J.P.7
  • 13
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • K. Diederichs, J. Diez, G. Greller, C. Muller, J. Breed, C. Schnell, C. Vonrhein, W. Boos, and W. Welte Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis EMBO J 19 2000 5951 5961
    • (2000) EMBO J , vol.19 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3    Muller, C.4    Breed, J.5    Schnell, C.6    Vonrhein, C.7    Boos8    Welte, W.W.9
  • 14
    • 0035801375 scopus 로고    scopus 로고
    • Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing
    • R. Gaudet, and D.C. Wiley Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing EMBO J 20 2001 4964 4972
    • (2001) EMBO J , vol.20 , pp. 4964-4972
    • Gaudet1    Wiley, D.C.R.2
  • 15
    • 0034941969 scopus 로고    scopus 로고
    • Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter
    • N. Karpowich, O. Martsinkevich, L. Millen, Y.R. Yuan, P.L. Dai, K. MacVey, P.J. Thomas, and J.F. Hunt Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter Structure 9 2001 571 586
    • (2001) Structure , vol.9 , pp. 571-586
    • Karpowich, N.1    Martsinkevich, O.2    Millen, L.3    Yuan, Y.R.4    Dai, P.L.5    MacVey, K.6    Thomas7    Hunt, J.F.P.J.8
  • 16
    • 0035943735 scopus 로고    scopus 로고
    • The crystal structure of the MJ0796 ATP-binding cassette - Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter
    • Y.R. Yuan, S. Blecker, O. Martsinkevich, L. Millen, P.J. Thomas, and J.F. Hunt The crystal structure of the MJ0796 ATP-binding cassette - implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter J Biol Chem 276 2001 32313 32321
    • (2001) J Biol Chem , vol.276 , pp. 32313-32321
    • Yuan, Y.R.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas5    Hunt, J.F.P.J.6
  • 17
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • P.C. Smith, N. Karpowich, L. Millen, J.E. Moody, J. Rosen, P.J. Thomas, and J.F. Hunt ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer Mol Cell 10 2002 139 149 This paper describes the crystal structure of a dimer of archaeal ABC domains trapped with bound ATP by using a Walker B mutation that abolishes ATPase activity. The structure visualizes an intermediate close to the transition state of the ATP hydrolysis reaction.
    • (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    Thomas6    Hunt, J.F.P.J.7
  • 18
    • 0038799733 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide-binding domain of the ABC transporter haemolysin B: Identification of a variable region within ABC helical domains
    • L. Schmitt, H. Benabdelhak, M.A. Blight, B.I. Holland, and M.T. Stubbs Crystal structure of the nucleotide-binding domain of the ABC transporter haemolysin B: identification of a variable region within ABC helical domains J Mol Biol 330 2003 333 342
    • (2003) J Mol Biol , vol.330 , pp. 333-342
    • Schmitt, L.1    Benabdelhak, H.2    Blight, M.A.3    Holland4    Stubbs, M.T.B.I.5
  • 19
    • 0038374988 scopus 로고    scopus 로고
    • Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: Nucleotide-free and nucleotide-bound conformations
    • G. Verdon, S.V. Albers, B.W. Dijkstra, A.J.M. Driessen, and A. Thunnissen Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations J Mol Biol 330 2003 343 358
    • (2003) J Mol Biol , vol.330 , pp. 343-358
    • Verdon, G.1    Albers, S.V.2    Dijkstra, B.W.3    Driessen4    Thunnissen, A.A.J.M.5
  • 20
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • J. Chen, G. Lu, J. Lin, A.L. Davidson, and F.A. Quiocho A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle Mol Cell 12 2003 651 661 This paper reveals the crystal structure of a homodimer of ABC domains (MalK) from the maltose importer system in three different conformations: open, semi-open and closed. In the open state, a gap is present between the ABC domains, whereas the regulatory domains remain in contact.
    • (2003) Mol Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson4    Quiocho, F.A.A.L.5
  • 22
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • P.M. Jones, and A.M. George Subunit interactions in ABC transporters: towards a functional architecture FEMS Microbiol Lett 179 1999 187 202
    • (1999) FEMS Microbiol Lett , vol.179 , pp. 187-202
    • Jones1    George, A.M.P.M.2
  • 23
    • 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
    • H.L. Chen, D. Gabrilovich, R. Tampe, K.R. Girgis, S. Nadaf, and D.P. Carbone A functionally defective allele of TAP1 results in loss of MHC class I antigen presentation in a human lung cancer Nat Genet 13 1996 210 213
    • (1996) Nat Genet , vol.13 , pp. 210-213
    • Chen, H.L.1    Gabrilovich, D.2    Tampe, R.3    Girgis, K.R.4    Nadaf5    Carbone, D.P.S.6
  • 24
    • 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
    • L. Saveanu, S. Daniel, and P.M. van Endert 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 2001 22107 22113
    • (2001) J Biol Chem , vol.276 , pp. 22107-22113
    • Saveanu, L.1    Daniel2    Van Endert, P.M.S.3
  • 25
    • 0027481813 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator
    • J.R. Riordan The cystic fibrosis transmembrane conductance regulator Annu Rev Physiol 55 1993 609 630
    • (1993) Annu Rev Physiol , vol.55 , pp. 609-630
    • Riordan, J.R.1
  • 26
    • 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
    • M. Mourez, N. Hofnung, and E. Dassa 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 1997 3066 3077
    • (1997) EMBO J , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung2    Dassa, E.N.3
  • 27
    • 0029835571 scopus 로고    scopus 로고
    • Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator
    • J.F. Cotten, L.S. Ostedgaard, M.R. Carson, and M.J. Welsh Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator J Biol Chem 271 1996 21279 21284
    • (1996) J Biol Chem , vol.271 , pp. 21279-21284
    • Cotten, J.F.1    Ostedgaard, L.S.2    Carson3    Welsh, M.J.M.R.4
  • 28
    • 0026473238 scopus 로고
    • Identification of residues in the 1st cytoplasmic loop of P-glycoprotein involved in the function of chimeric human Mdr1- Mdr2 transporters
    • S.J. Currier, S.E. Kane, M.C. Willingham, C.O. Cardarelli, I. Pastan, and M.M. Gottesman Identification of residues in the 1st cytoplasmic loop of P-glycoprotein involved in the function of chimeric human Mdr1- Mdr2 transporters J Biol Chem 267 1992 25153 25159
    • (1992) J Biol Chem , vol.267 , pp. 25153-25159
    • Currier, S.J.1    Kane, S.E.2    Willingham, M.C.3    Cardarelli, C.O.4    Pastan5    Gottesman, M.M.I.6
  • 29
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • F.A. Quiocho, and P.S. Ledvina Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes Mol Microbiol 20 1996 17 25
    • (1996) Mol Microbiol , vol.20 , pp. 17-25
    • Quiocho1    Ledvina, P.S.F.A.2
  • 30
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • D.P. Chimento, A.K. Mohanty, R.J. Kadner, and M.C. Wiener Substrate-induced transmembrane signaling in the cobalamin transporter BtuB Nat Struct Biol 10 2003 394 401
    • (2003) Nat Struct Biol , vol.10 , pp. 394-401
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner3    Wiener, M.C.R.J.4
  • 32
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • J. Chen, S. Sharma, F.A. Quiocho, and A.L. Davidson Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport Proc Natl Acad Sci USA 98 2001 1525 1530
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho3    Davidson, A.L.F.A.4
  • 34
    • 0037424343 scopus 로고    scopus 로고
    • Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding
    • M.F. Rosenberg, A.B. Kamis, R. Callaghan, C.F. Higgins, and R.C. Ford Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding J Biol Chem 278 2003 8294 8299
    • (2003) J Biol Chem , vol.278 , pp. 8294-8299
    • Rosenberg, M.F.1    Kamis, A.B.2    Callaghan, R.3    Higgins4    Ford, R.C.C.F.5
  • 35
    • 0034765259 scopus 로고    scopus 로고
    • A snapshot of Nature's favorite pump
    • P.J. Thomas, and J.F. Hunt A snapshot of Nature's favorite pump Nat Struct Biol 8 2001 920 923
    • (2001) Nat Struct Biol , vol.8 , pp. 920-923
    • Thomas1    Hunt, J.F.P.J.2
  • 36
    • 0036179213 scopus 로고    scopus 로고
    • Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters
    • A.L. Davidson Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters J Bacteriol 184 2002 1225 1233
    • (2002) J Bacteriol , vol.184 , pp. 1225-1233
    • Davidson, A.L.1
  • 37
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • J.E. Moody, L. Millen, D. Binns, J.F. Hunt, and P.J. Thomas Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters J Biol Chem 277 2002 21111 21114
    • (2002) J Biol Chem , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt4    Thomas, P.J.J.F.5
  • 38
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • J. Abramson, I. Smirnova, V. Kasho, G. Verner, H.R. Kaback, and S. Iwata Structure and mechanism of the lactose permease of Escherichia coli Science 301 2003 610 615 The first crystal structure of the E. coli lactose permease LacY. The results and relevance are discussed in the review by Abramson, Kaback and Iwata in this issue.
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback5    Iwata, S.H.R.6
  • 39
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Y.F. Huang, M.J. Lemieux, J.M. Song, M. Auer, and D.N. Wang Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli Science 301 2003 616 620 The first crystal structure of the E. coli glycerol-3-phosphate transporter GlpT. The results and relevance are discussed in the review by Lemieux, Huang and Wang in this issue.
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.F.1    Lemieux, M.J.2    Song, J.M.3    Auer4    Wang, D.N.M.5
  • 40
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • J.S. Patzlaff, T. van der Heide, and B. Poolman The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA J Biol Chem 278 2003 29546 29551
    • (2003) J Biol Chem , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    Der Heide, V.2    Poolman, B.T.3


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