메뉴 건너뛰기




Volumn 10, Issue 3, 2009, Pages 218-227

ABC transporters: The power to change

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; NUCLEOTIDE;

EID: 60749083913     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2646     Document Type: Review
Times cited : (1064)

References (80)
  • 2
    • 33646405732 scopus 로고    scopus 로고
    • The biological frontier of physics
    • Phillips, R. & Quake, S. R. The biological frontier of physics. Phys. Today 59, 38-43 (2006).
    • (2006) Phys. Today , vol.59 , pp. 38-43
    • Phillips, R.1    Quake, S.R.2
  • 3
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F. R. et al. The complete genome sequence of Escherichia coli K-12. Science 277, 1453-1462 (1997).
    • (1997) Science , vol.277 , pp. 1453-1462
    • Blattner, F.R.1
  • 5
    • 0001833934 scopus 로고
    • The search for correlation between theoretical and experimental growth yields
    • Stouthamer, A. H. The search for correlation between theoretical and experimental growth yields. Int. Rev. Biochem. 21, 1-47 (1979).
    • (1979) Int. Rev. Biochem , vol.21 , pp. 1-47
    • Stouthamer, A.H.1
  • 6
    • 60749121789 scopus 로고    scopus 로고
    • Neijsel, O. M., Teixeira de Mattos, M. J. & Tempest, D. W. in Escherichia coli and Salmonella: Cellular and Molecular Biology (ed. Neidhardt, F. C.) 1283-1692 (ASM, Washington DC, 1996).
    • Neijsel, O. M., Teixeira de Mattos, M. J. & Tempest, D. W. in Escherichia coli and Salmonella: Cellular and Molecular Biology (ed. Neidhardt, F. C.) 1283-1692 (ASM, Washington DC, 1996).
  • 7
    • 0032544666 scopus 로고    scopus 로고
    • The identification of the sodium-potassium pump (Nobel lecture)
    • Skou, J. C. The identification of the sodium-potassium pump (Nobel lecture). Angew. Chem. Int. Edn Eng. 37, 2320-2328 (1998).
    • (1998) Angew. Chem. Int. Edn Eng , vol.37 , pp. 2320-2328
    • Skou, J.C.1
  • 8
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8, 67-113 (1992).
    • (1992) Annu. Rev. Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 9
    • 0026472873 scopus 로고
    • Traffic ATPases: A superfamily of transport proteins operating from Escherichia coli to humans
    • Ames, G. F., Mimura, C. S., Holbrook, S. R. & Shyamala, V. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv. Enzymol. Relat. Areas Mol. Biol. 65, 1-47 (1992).
    • (1992) Adv. Enzymol. Relat. Areas Mol. Biol , vol.65 , pp. 1-47
    • Ames, G.F.1    Mimura, C.S.2    Holbrook, S.R.3    Shyamala, V.4
  • 10
    • 85163545088 scopus 로고    scopus 로고
    • Holland, I. B, Cole, S. P. C, Kuchler, K. & Higgins, C. F, eds, Academic, London
    • Holland, I. B., Cole, S. P. C., Kuchler, K. & Higgins, C. F. (eds) ABC proteins: From Bacteria to Man (Academic, London, 2003).
    • (2003) ABC proteins: From Bacteria to Man
  • 11
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton, K. J. & Higgins, C. F. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28, 5-13 (1998).
    • (1998) Mol. Microbiol , vol.28 , pp. 5-13
    • Linton, K.J.1    Higgins, C.F.2
  • 12
    • 0034917716 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • Dean, M., Rzhetsky, A. & Allikmets, R. The human ATP-binding cassette (ABC) transporter superfamily. Genome Res. 11, 1156-1166 (2001).
    • (2001) Genome Res , vol.11 , pp. 1156-1166
    • Dean, M.1    Rzhetsky, A.2    Allikmets, R.3
  • 13
    • 25844487733 scopus 로고    scopus 로고
    • Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates
    • Dean, M. & Annilo, T. Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates. Annu. Rev. Genomics Hum. Genet. 6, 123-142 (2005).
    • (2005) Annu. Rev. Genomics Hum. Genet , vol.6 , pp. 123-142
    • Dean, M.1    Annilo, T.2
  • 14
    • 31944431842 scopus 로고    scopus 로고
    • ABC transporter architecture and regulatory roles of accessory domains
    • Biemans-Oldehinkel, E., Deoven, M. K. & Poolman, B. ABC transporter architecture and regulatory roles of accessory domains. FEBS Lett. 580, 1023-1035 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 1023-1035
    • Biemans-Oldehinkel, E.1    Deoven, M.K.2    Poolman, B.3
  • 15
    • 0022555851 scopus 로고
    • Bacterial periplasmic transport systems - structure, mechanism and evolution
    • Ames, G. F. L. Bacterial periplasmic transport systems - structure, mechanism and evolution. Annu. Rev. Biochem. 55, 397-425 (1986).
    • (1986) Annu. Rev. Biochem , vol.55 , pp. 397-425
    • Ames, G.F.L.1
  • 16
    • 1842340069 scopus 로고
    • The effect of osmotic shock on release of bacterial proteins and on active transport
    • Heppel, L. A. The effect of osmotic shock on release of bacterial proteins and on active transport. J. Gen. Physiol. 54, 95-113 (1969).
    • (1969) J. Gen. Physiol , vol.54 , pp. 95-113
    • Heppel, L.A.1
  • 17
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • The first crystal structure of an intact ABC transporter, the vitamin B12 importer BtuCD
    • Locher, K. P., Lee, A. T. & Rees, D. C. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296, 1091-1098 (2002). The first crystal structure of an intact ABC transporter, the vitamin B12 importer BtuCD.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 18
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • The first crystal structure of an ABC exporter, the bacterial multidrug transporter Sav1866
    • Dawson, R. J. P. & Locher, K. P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006). The first crystal structure of an ABC exporter, the bacterial multidrug transporter Sav1866.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 19
    • 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. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 581, 935-938 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 935-938
    • Dawson, R.J.P.1    Locher, K.P.2
  • 20
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate type ABC transporter
    • The crystal structure of a BtuCD homologue exhibiting an inward-facing conformation
    • Pinkett, H. W., Lee, A. T., Lum, P., Locher, K. P. & Rees, D. C. An inward-facing conformation of a putative metal-chelate type ABC transporter. Science 315, 373-377 (2007). The crystal structure of a BtuCD homologue exhibiting an inward-facing conformation.
    • (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
  • 21
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter binding protein complex BtuCD-BtuF
    • The crystal structure of BtuCD complexed to the binding protein BtuF adopts an asymmetric conformation around the translocation pathway
    • Hvorup, R. N. et al. Asymmetry in the structure of the ABC transporter binding protein complex BtuCD-BtuF. Science 317, 1387-1390 (2007). The crystal structure of BtuCD complexed to the binding protein BtuF adopts an asymmetric conformation around the translocation pathway.
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1
  • 22
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • The first structure of a complex between an ABC transporter, ModBC, and its associated binding protein, ModA
    • Hollenstein, K., Frei, D. C. & Locher, K. P. Structure of an ABC transporter in complex with its binding protein. Nature 446, 213-216 (2007). The first structure of a complex between an ABC transporter, ModBC, and its associated binding protein, ModA.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 23
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • The structure of the maltose ABC transporter-binding protein complex in the ATP-bound state with a maltose trapped in its translocation pathway
    • Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L. & Chen, J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515-522 (2007). The structure of the maltose ABC transporter-binding protein complex in the ATP-bound state with a maltose trapped in its translocation pathway.
    • (2007) Nature , vol.450 , pp. 515-522
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 24
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Structures of the bacterial multidrug transporter homologue MsbA in different conformational states
    • Ward, A., Reyes, C. L., Yu, J., Roth, C. B. & Chang, G. Flexibility in the ABC transporter MsbA: alternating access with a twist. Proc. Natl Acad. Sci. USA 104, 19005-19010 (2007). Structures of the bacterial multidrug transporter homologue MsbA in different conformational states.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 25
    • 47249110343 scopus 로고    scopus 로고
    • Gerber, S., Comellas-Bigler, M., Goetz, B. A. & Locher, K. P. Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321, 246-250 (2008). The binding of molybdate and tungstate to regulatory domains of the ABC subunits stabilizes an inward-facing, ATPase-inactive conformation of a ModBC transporter that underllies the phenomenon of trans-inhibition.
    • Gerber, S., Comellas-Bigler, M., Goetz, B. A. & Locher, K. P. Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321, 246-250 (2008). The binding of molybdate and tungstate to regulatory domains of the ABC subunits stabilizes an inward-facing, ATPase-inactive conformation of a ModBC transporter that underllies the phenomenon of trans-inhibition.
  • 26
    • 47249084799 scopus 로고    scopus 로고
    • Kadaba, N. S., Kaiser, J. T., Johnson, E., Lee, A. & Rees, D. C. The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321, 250-253 (2008). The binding of Met to regulatory domains of the ABC subunits stabilizes an inward-facing, ATPase-inactive conformation of a MetNI transporter underlying the phenomenon of trans-inhibition.
    • Kadaba, N. S., Kaiser, J. T., Johnson, E., Lee, A. & Rees, D. C. The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321, 250-253 (2008). The binding of Met to regulatory domains of the ABC subunits stabilizes an inward-facing, ATPase-inactive conformation of a MetNI transporter underlying the phenomenon of trans-inhibition.
  • 28
    • 34247123807 scopus 로고    scopus 로고
    • Structure and function of ABC transporters
    • Linton, K. J. Structure and function of ABC transporters. Physiology (Bethesda) 22, 122-130 (2007).
    • (2007) Physiology (Bethesda) , vol.22 , pp. 122-130
    • Linton, K.J.1
  • 29
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson, A. L., Dassa, E., Orelle, C. & Chen, J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72, 317-364 (2008).
    • (2008) Microbiol. Mol. Biol. Rev , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 30
    • 35648963623 scopus 로고    scopus 로고
    • ABC transporters: How small molecules do a big job
    • Davidson, A. L. & Maloney, P. C. ABC transporters: how small molecules do a big job. Trends Microbiol. 15, 448-455 (2007).
    • (2007) Trends Microbiol , vol.15 , pp. 448-455
    • Davidson, A.L.1    Maloney, P.C.2
  • 31
    • 34447311648 scopus 로고    scopus 로고
    • Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism
    • Dawson, R. J. P., Hollenstein, K. & Locher, K. P. Uptake or extrusion: crystal structures of full ABC transporters suggest a common mechanism. Mol. Microbiol. 65, 250-257 (2007).
    • (2007) Mol. Microbiol , vol.65 , pp. 250-257
    • Dawson, R.J.P.1    Hollenstein, K.2    Locher, K.P.3
  • 32
    • 57049124822 scopus 로고    scopus 로고
    • Structural insights into ABC transporter mechanism
    • Oldham, M. L., Davidson, A. L. & Chen, J. Structural insights into ABC transporter mechanism. Curr. Opin. Struct. Biol. 18, 726-733 (2008).
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 726-733
    • Oldham, M.L.1    Davidson, A.L.2    Chen, J.3
  • 33
    • 61449341855 scopus 로고    scopus 로고
    • Structure and mechanism of ATP-binding cassette transporters
    • Locher, K. P. Structure and mechanism of ATP-binding cassette transporters. Phil. Trans. R. Soc. Lond. B 364, 239-245 (2008).
    • (2008) Phil. Trans. R. Soc. Lond. B , vol.364 , pp. 239-245
    • Locher, K.P.1
  • 34
    • 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
    • Schmitt, L., Benabdelhak, H., Blight, M. A., Holland, I. B. & Stubbs, M. T. 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, 333-342 (2003).
    • (2003) J. Mol. Biol , vol.330 , pp. 333-342
    • Schmitt, L.1    Benabdelhak, H.2    Blight, M.A.3    Holland, I.B.4    Stubbs, M.T.5
  • 35
    • 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
    • Karpowich, N. et al. Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Structure 9, 571-586 (2001).
    • (2001) Structure , vol.9 , pp. 571-586
    • Karpowich, N.1
  • 36
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • Jones, P. M. & George, A. M. Subunit interactions in ABC transporters: towards a functional architecture. FEMS Microbiol. Lett. 179, 187-202 (1999).
    • (1999) FEMS Microbiol. Lett , vol.179 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 37
    • 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. et al. 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).
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.-P.1
  • 38
    • 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. et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1
  • 39
    • 0028240216 scopus 로고
    • Bacterial binding protein-dependent permeases - characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins
    • Saurin, W., Koster, W. & Dassa, E. Bacterial binding protein-dependent permeases - characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 12, 993-1004 (1994).
    • (1994) Mol. Microbiol , vol.12 , pp. 993-1004
    • Saurin, W.1    Koster, W.2    Dassa, E.3
  • 40
    • 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. 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).
    • (1997) EMBO J , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, N.2    Dassa, E.3
  • 41
    • 0036789902 scopus 로고    scopus 로고
    • Mechanism of ABC transporters: A molecular dynamics simulation of a well characterized nucleotide-binding subunit
    • Jones, P. M. & George, A. M. Mechanism of ABC transporters: a molecular dynamics simulation of a well characterized nucleotide-binding subunit. Proc. Natl Acad. Sci. USA 99, 12639-12644 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12639-12644
    • Jones, P.M.1    George, A.M.2
  • 42
    • 0035014565 scopus 로고    scopus 로고
    • The ABC of ABCs: A phylogenetic and functional classification of ABC systems in living organisms
    • Dassa, E. & Bouige, E. The ABC of ABCs: a phylogenetic and functional classification of ABC systems in living organisms. Res. Microbiol. 152, 211-229 (2001).
    • (2001) Res. Microbiol , vol.152 , pp. 211-229
    • Dassa, E.1    Bouige, E.2
  • 43
    • 0041387450 scopus 로고    scopus 로고
    • Topology of RbsC, the membrane component of the Escherichia coli ribose transporter
    • Steward, J. B. & Hermodson, M. A. Topology of RbsC, the membrane component of the Escherichia coli ribose transporter. J. Bacteriol. 185, 5234-5239 (2003).
    • (2003) J. Bacteriol , vol.185 , pp. 5234-5239
    • Steward, J.B.1    Hermodson, M.A.2
  • 44
    • 0033548125 scopus 로고    scopus 로고
    • Domain dislocation: A change of core structure in periplasmic binding proteins in their evolutionary history
    • Fukami-Kobayashi, K., Tateno, Y. & Nishikawa, K. Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history. J. Mol. Biol. 286, 279-290 (1999).
    • (1999) J. Mol. Biol , vol.286 , pp. 279-290
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 45
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variations of common themes
    • Quiocho, F. A. & Ledvina, P. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variations of common themes. Mol. Microbiol. 20, 17-25 (1996).
    • (1996) Mol. Microbiol , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.2
  • 47
    • 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, W. F. 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, 23-39 (1952).
    • (1952) J. Physiol , vol.118 , pp. 23-39
    • Widdas, W.F.1
  • 48
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetsky, O. Simple allosteric model for membrane pumps. Nature 211, 969-970 (1966).
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetsky, O.1
  • 49
    • 28944449620 scopus 로고    scopus 로고
    • Functional analysis of detergent solubilized and membrane-reconstituted ABC transporters
    • Poolman, B. et al. Functional analysis of detergent solubilized and membrane-reconstituted ABC transporters. Methods Enzymol. 400, 429-459 (2005).
    • (2005) Methods Enzymol , vol.400 , pp. 429-459
    • Poolman, B.1
  • 50
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • A careful measurement of the ATP-to-translocated ligand ratio for the tightly coupled OpuA transporter
    • Patzlaff, J. S., van der Heide, T. & Poolman, B. The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA. J. Biol. Chem. 278, 29546-29551 (2003). A careful measurement of the ATP-to-translocated ligand ratio for the tightly coupled OpuA transporter.
    • (2003) J. Biol. Chem , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    van der Heide, T.2    Poolman, B.3
  • 51
    • 0025214263 scopus 로고
    • Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli
    • Davidson, A. L. & Nikaido, H. Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli. J. Biol. Chem. 265, 4254-4260 (1990).
    • (1990) J. Biol. Chem , vol.265 , pp. 4254-4260
    • Davidson, A.L.1    Nikaido, H.2
  • 52
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • ATP-vanadate is used to trap a complex between the maltose transporter and the binding protein
    • Chen, J., Sharma, S., Quiocho, F. A. & Davidson, A. L. 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). ATP-vanadate is used to trap a complex between the maltose transporter and the binding protein.
    • (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
  • 54
    • 0033578760 scopus 로고    scopus 로고
    • One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease
    • Nikaido, K. & Ames, G. F. L. One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease. J. Biol. Chem. 274, 26727-26735 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 26727-26735
    • Nikaido, K.1    Ames, G.F.L.2
  • 55
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP-synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. Distantly related sequences in the α- and β-subunits of ATP-synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951 (1982).
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 56
    • 0029781354 scopus 로고    scopus 로고
    • Ras-catalyzed hydrolysis of GTP: A new perspective from model studies
    • Maegley, K. A., Admiraal, S. J. & Herschlag, D. Ras-catalyzed hydrolysis of GTP: a new perspective from model studies. Proc. Natl Acad. Sci. USA 93, 8160-8166 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8160-8166
    • Maegley, K.A.1    Admiraal, S.J.2    Herschlag, D.3
  • 57
    • 0032522882 scopus 로고    scopus 로고
    • How do kinases transfer phosphoryl groups?
    • Matte, A., Tari, L. W. & Delbaere, L. T. J. How do kinases transfer phosphoryl groups? Structure 6, 413-419 (1998).
    • (1998) Structure , vol.6 , pp. 413-419
    • Matte, A.1    Tari, L.W.2    Delbaere, L.T.J.3
  • 58
    • 0035449570 scopus 로고    scopus 로고
    • A common mechanism for ATP hydrolysis in ABC transporter and helicase superfamilies
    • Geourjon, C. et al. A common mechanism for ATP hydrolysis in ABC transporter and helicase superfamilies. Trends Biochem. Sci. 25, 539-544 (2001).
    • (2001) Trends Biochem. Sci , vol.25 , pp. 539-544
    • Geourjon, C.1
  • 59
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding casettes during the catalytic cycle of ATP-binding cassette transporters
    • Moody, J. E., Millen., L., Binns, D., Hunt, J. F. & Thomas, P. J. Cooperative, ATP-dependent association of the nucleotide binding casettes during the catalytic cycle of ATP-binding cassette transporters. J. Biol. Chem. 277, 21111-21114 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 60
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva, J. et al. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24, 1901-1910 (2005).
    • (2005) EMBO J , vol.24 , pp. 1901-1910
    • Zaitseva, J.1
  • 61
    • 0035838982 scopus 로고    scopus 로고
    • Structure of bovine mitochondrial F1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • Menz, R. I., Walker, J. E. & Leslie, A. G. W. Structure of bovine mitochondrial F1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 106, 331-341 (2001).
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.W.3
  • 63
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe, D. D., Koonin, E. V. & Aravind, L. Evolution and classification of P-loop kinases and related proteins. J. Mol. Biol. 333, 781-815 (2003).
    • (2003) J. Mol. Biol , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 65
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: Structural basis for GTPase activation and its loss in oncogenic Ras mutants
    • Scheffzek, K. et al. The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277, 333-338 (1997).
    • (1997) Science , vol.277 , pp. 333-338
    • Scheffzek, K.1
  • 67
    • 0031282504 scopus 로고    scopus 로고
    • Signaling mechanistics: Aluminum fluoride for molecule of the year
    • Wittinghofer, A. Signaling mechanistics: aluminum fluoride for molecule of the year. Curr. Biol. 7, R682-R685 (1997).
    • (1997) Curr. Biol , vol.7
    • Wittinghofer, A.1
  • 68
    • 0032751576 scopus 로고    scopus 로고
    • Structural bioenergetics and energy transduction mechanisms
    • Rees, D. C. & Howard, J. B. Structural bioenergetics and energy transduction mechanisms. J. Mol. Biol. 293, 343-350 (1999).
    • (1999) J. Mol. Biol , vol.293 , pp. 343-350
    • Rees, D.C.1    Howard, J.B.2
  • 69
    • 0141527345 scopus 로고    scopus 로고
    • Chen, J., Lu, G., Lin, J., Davidson, A. L. & Quiocho, F. A. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12, 651-661 (2003).
    • Chen, J., Lu, G., Lin, J., Davidson, A. L. & Quiocho, F. A. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12, 651-661 (2003).
  • 70
    • 51349104365 scopus 로고    scopus 로고
    • Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter
    • Orelle, C., Ayvaz, T., Everly, R. M., Klug, C. S. & Davidson, A. L. Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter. Proc. Natl Acad. Sci. USA 105, 12837-12842 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 12837-12842
    • Orelle, C.1    Ayvaz, T.2    Everly, R.M.3    Klug, C.S.4    Davidson, A.L.5
  • 71
    • 58149512047 scopus 로고    scopus 로고
    • Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking
    • Goetz, B. A., Perozo, E. & Locher, K. P. Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking. FEBS Lett. 583, 266-270 (2009).
    • (2009) FEBS Lett , vol.583 , pp. 266-270
    • Goetz, B.A.1    Perozo, E.2    Locher, K.P.3
  • 72
    • 0016671558 scopus 로고    scopus 로고
    • Kadner, R. J. Regulation of methionine transport activity in Escherichia coli. J. Bacteriol. 122, 110-119 (1975). An exquisite in vivo analysis of the trans-inhibition of Met transport activity by intracellular Met.
    • Kadner, R. J. Regulation of methionine transport activity in Escherichia coli. J. Bacteriol. 122, 110-119 (1975). An exquisite in vivo analysis of the trans-inhibition of Met transport activity by intracellular Met.
  • 73
    • 54449097276 scopus 로고    scopus 로고
    • ATP hydrolysis and pristinamycin IIA inhibition of the Staphylococcus aureus Vga(A), a dual ABC protein involved in streptogramin A resistance
    • Jacquet, E. et al. ATP hydrolysis and pristinamycin IIA inhibition of the Staphylococcus aureus Vga(A), a dual ABC protein involved in streptogramin A resistance. J. Biol. Chem. 283, 25332-25339 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 25332-25339
    • Jacquet, E.1
  • 74
    • 0037398027 scopus 로고    scopus 로고
    • Rad50/SMC proteins and ABC transporters: Unifying concepts from high-resolution structures
    • Hopfner, K. P. & Tainer, J. A. Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures. Curr. Opin. Struct. Biol. 13, 249-255 (2003).
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 249-255
    • Hopfner, K.P.1    Tainer, J.A.2
  • 76
    • 34147214716 scopus 로고    scopus 로고
    • Multiple molecular mechanisms for multidrug resistance transporters
    • Higgins, C. F. Multiple molecular mechanisms for multidrug resistance transporters. Nature 446, 749-757 (2007).
    • (2007) Nature , vol.446 , pp. 749-757
    • Higgins, C.F.1
  • 77
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 78
    • 0028057108 scopus 로고    scopus 로고
    • Merritt, E. A. & Murphy, M. E. P. Raster3D Version 2.0, a program for photorealistic molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 50, 869-873 1994
    • Merritt, E. A. & Murphy, M. E. P. Raster3D Version 2.0 - a program for photorealistic molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 50, 869-873 (1994).
  • 79
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman, H. M. et al. The Protein Data Bank. Nucleic Acids Res. 28, 235-242 (2000).
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 80
    • 0042844976 scopus 로고    scopus 로고
    • 4-stabilized structure
    • 4-stabilized structure. Biochemistry 41, 15557-15565 (2002).
    • (2002) Biochemistry , vol.41 , pp. 15557-15565
    • Schmid, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.