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Volumn 564, Issue 3, 2004, Pages 264-268

ABC transporter architecture and mechanism: Implications from the crystal structures of BtuCD and BtuF

Author keywords

ABC transporter; Crystal structure; Transport mechanism

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; CYANOCOBALAMIN BINDING PROTEIN; MEMBRANE PROTEIN; PERIPLASMIC BINDING PROTEIN; PROTEIN SUBUNIT;

EID: 1942532335     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(04)00289-3     Document Type: Conference Paper
Times cited : (43)

References (34)
  • 1
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: Physiology, structure and mechanism - An overview
    • Higgins C.F. ABC transporters: physiology, structure and mechanism - an overview. Res. Microbiol. 152:2001;205-210.
    • (2001) Res. Microbiol. , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 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
    • Saurin W., Hofnung M., Dassa E. 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    Hofnung, M.2    Dassa, E.3
  • 3
    • 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. 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
    • Schneider, E.1    Hunke, S.2
  • 4
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules organisms from bacteria to humans
    • Holland I.B., Blight M.A. 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
    • Holland, I.B.1    Blight, M.A.2
  • 5
    • 0035685449 scopus 로고    scopus 로고
    • Complete characterization of the human ABC gene family
    • Dean M., Allikmets R. Complete characterization of the human ABC gene family. J. Bioenerg. Biomembr. 33:2001;475-479.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 475-479
    • Dean, M.1    Allikmets, R.2
  • 6
    • 0032323640 scopus 로고    scopus 로고
    • Overview of bacterial ABC transporters
    • Nikaido H., Hall J.A. Overview of bacterial ABC transporters. Methods Enzymol. 292:1998;3-20.
    • (1998) Methods Enzymol. , vol.292 , pp. 3-20
    • Nikaido, H.1    Hall, J.A.2
  • 7
    • 0032742380 scopus 로고    scopus 로고
    • ABC transporters: Bacterial exporters - Revisited five years on
    • Young J., Holland I.B. ABC transporters: bacterial exporters - revisited five years on. Biochim. Biophys. Acta. 1461:1999;177-200.
    • (1999) Biochim. Biophys. Acta , vol.1461 , pp. 177-200
    • Young, J.1    Holland, I.B.2
  • 8
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst P., Elferink R.O. Mammalian ABC transporters in health and disease. Annu. Rev. Biochem. 71:2002;537-592.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 537-592
    • Borst, P.1    Elferink, R.O.2
  • 9
    • 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. 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    Ames, G.F.L.5    Kim, S.H.6
  • 10
    • 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. 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    Carney, J.P.6    Tainer, J.A.7
  • 11
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs K., Diez J., Greller G., Muller C., Breed J., Schnell C., Vonrhein C., Boos W., Welte W. 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    Boos, W.8    Welte, W.9
  • 12
    • 0035801375 scopus 로고    scopus 로고
    • Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing
    • Gaudet R., Wiley D.C. 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
    • Gaudet, R.1    Wiley, D.C.2
  • 13
    • 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., Martsinkevich O., Millen L., Yuan Y.R., Dai P.L., MacVey K., Thomas P.J., Hunt J.F. 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    Thomas, P.J.7    Hunt, J.F.8
  • 14
    • 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
    • Yuan Y.R., Blecker S., Martsinkevich O., Millen L., Thomas P.J., Hunt J.F. 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    Thomas, P.J.5    Hunt, J.F.6
  • 15
    • 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. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell. 10:2002;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
  • 16
    • 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 B.I., 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. 330:2003;333-342.
    • (2003) J. Mol. Biol. , vol.330 , pp. 333-342
    • Schmitt, L.1    Benabdelhak, H.2    Blight, M.A.3    Holland, B.I.4    Stubbs, M.T.5
  • 17
    • 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
    • Verdon G., Albers S.V., Dijkstra B.W., Driessen A.J.M., Thunnissen A. 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    Driessen, A.J.M.4    Thunnissen, A.5
  • 18
    • 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. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell. 12:2003;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
  • 20
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang G., Roth C.B. 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
    • Chang, G.1    Roth, C.B.2
  • 21
    • 0038799725 scopus 로고    scopus 로고
    • Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation
    • Chang G. Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation. J. Mol. Biol. 330:2003;419-430.
    • (2003) J. Mol. Biol. , vol.330 , pp. 419-430
    • Chang, G.1
  • 22
    • 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. The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism. Science. 296:2002;1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 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
    • Chen H.L., Gabrilovich D., Tampe R., Girgis K.R., Nadaf S., Carbone D.P. 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    Nadaf, S.5    Carbone, D.P.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
    • Saveanu L., Daniel S., van Endert P.M. 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    Daniel, S.2    Van Endert, P.M.3
  • 25
    • 0027481813 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator
    • Riordan J.R. 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
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • Chimento D.P., Mohanty A.K., Kadner R.J., Wiener M.C. 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    Kadner, R.J.3    Wiener, M.C.4
  • 28
    • 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. The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proc. Natl. Acad. Sci. USA. 99:2002;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
  • 29
    • 0037424465 scopus 로고    scopus 로고
    • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding
    • Karpowich N.K., Huang H.H., Smith P.C., Hunt J.F. Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding. J. Biol. Chem. 278:2003;8429-8434.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 30
    • 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. 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    Quiocho, F.A.3    Davidson, A.L.4
  • 32
    • 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
    • Rosenberg M.F., Kamis A.B., Callaghan R., Higgins C.F., Ford R.C. 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    Higgins, C.F.4    Ford, R.C.5
  • 33
    • 0036179213 scopus 로고    scopus 로고
    • Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters
    • Davidson A.L. 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
  • 34
    • 0034765259 scopus 로고    scopus 로고
    • A snapshot of Nature's favorite pump
    • Thomas P.J., Hunt J.F. A snapshot of Nature's favorite pump. Nat. Struct. Biol. 8:2001;920-923.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 920-923
    • Thomas, P.J.1    Hunt, J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.