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Volumn 17, Issue 9, 2009, Pages 1213-1222

Insights into How Nucleotide-Binding Domains Power ABC Transport

Author keywords

CELLBIO; PROTEINS

Indexed keywords

ABC TRANSPORTER; FERRIC ION; NUCLEOTIDE; PROTEIN MALK; UNCLASSIFIED DRUG;

EID: 69949136235     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.07.009     Document Type: Article
Times cited : (42)

References (60)
  • 3
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: a snapshot of the evolution of sequence, structure and function
    • Arcus V. OB-fold domains: a snapshot of the evolution of sequence, structure and function. Curr. Opin. Struct. Biol. 12 (2002) 794-801
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 794-801
    • Arcus, V.1
  • 6
    • 22544453328 scopus 로고    scopus 로고
    • Nucleotide binding to the homodimeric MJ0796 protein: A computational study of a prokaryotic ABC transporter NBD dimer
    • Campbell J.D., and Sansom M.S.P. Nucleotide binding to the homodimeric MJ0796 protein: A computational study of a prokaryotic ABC transporter NBD dimer. FEBS Lett. 579 (2005) 4193-4199
    • (2005) FEBS Lett. , vol.579 , pp. 4193-4199
    • Campbell, J.D.1    Sansom, M.S.P.2
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 8
    • 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., and 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
  • 9
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh Ewald: An N-log(N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 10
    • 0025214263 scopus 로고
    • Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli
    • Davidson A.L., and Nikaido H. Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli. J. Biol. Chem. 265 (1990) 4254-4260
    • (1990) J. Biol. Chem. , vol.265 , pp. 4254-4260
    • Davidson, A.L.1    Nikaido, H.2
  • 11
    • 0029868327 scopus 로고    scopus 로고
    • The maltose transport system of Escherichia coli displays positive cooperativity in ATP hydrolysis
    • Davidson A.L., Laghaeian S.S., and Mannering D.E. The maltose transport system of Escherichia coli displays positive cooperativity in ATP hydrolysis. J. Biol. Chem. 271 (1996) 4858-4863
    • (1996) J. Biol. Chem. , vol.271 , pp. 4858-4863
    • Davidson, A.L.1    Laghaeian, S.S.2    Mannering, D.E.3
  • 13
    • 69949182002 scopus 로고    scopus 로고
    • Palo Alto, CA: DeLano Scientific
    • DeLano, W.L. (2008). The PyMol Molecular Graphics System (Palo Alto, CA: DeLano Scientific) http://www.pymol.org.
    • (2008)
    • DeLano, W.L.1
  • 14
    • 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., and 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
  • 16
    • 0348244547 scopus 로고    scopus 로고
    • All-atom empircal force field for nucleic acids: I. Parameter optimization based on small molecule and condensed phase macromolecular target data
    • Foloppe N., and MacKerell Jr. A.D. All-atom empircal force field for nucleic acids: I. Parameter optimization based on small molecule and condensed phase macromolecular target data. J. Comput. Chem. 21 (2000) 86-104
    • (2000) J. Comput. Chem. , vol.21 , pp. 86-104
    • Foloppe, N.1    MacKerell Jr., A.D.2
  • 17
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • Gadsby D.C., Vergani P., and Csanady L. The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature 440 (2006) 477-483
    • (2006) Nature , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanady, L.3
  • 18
    • 47249110343 scopus 로고    scopus 로고
    • Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter
    • Gerber S., Comellas-Bigler M., Goetz B.A., and Locher K.P. Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321 (2008) 246-250
    • (2008) Science , vol.321 , pp. 246-250
    • Gerber, S.1    Comellas-Bigler, M.2    Goetz, B.A.3    Locher, K.P.4
  • 20
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins C.F., and Linton K.J. The ATP switch model for ABC transporters. Nat. Struct. Mol. Biol. 11 (2004) 918-926
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 22
    • 0038711772 scopus 로고    scopus 로고
    • The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p
    • Janas E., Hofacker M., Chen M., Gompf S., van der Does C., and Tampe R. The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J. Biol. Chem. 278 (2003) 26862-26869
    • (2003) J. Biol. Chem. , vol.278 , pp. 26862-26869
    • Janas, E.1    Hofacker, M.2    Chen, M.3    Gompf, S.4    van der Does, C.5    Tampe, R.6
  • 23
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O. Simple allosteric model for membrane pumps. Nature 211 (1966) 969-970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 24
    • 34547943910 scopus 로고    scopus 로고
    • Nucleotide-dependent Allostery within the ABC Transporter ATP-binding Cassette
    • Jones P.M., and George A.M. Nucleotide-dependent Allostery within the ABC Transporter ATP-binding Cassette. J. Biol. Chem. 282 (2007) 22793-22803
    • (2007) J. Biol. Chem. , vol.282 , pp. 22793-22803
    • Jones, P.M.1    George, A.M.2
  • 25
    • 66149139241 scopus 로고    scopus 로고
    • Opening of the ADP-bound active site in the ABC transporter ATPase dimer: evidence for a constant contact, alternating sites model for the catalytic cycle
    • Jones P.M., and George A.M. Opening of the ADP-bound active site in the ABC transporter ATPase dimer: evidence for a constant contact, alternating sites model for the catalytic cycle. Proteins 75 (2009) 387-396
    • (2009) Proteins , vol.75 , pp. 387-396
    • Jones, P.M.1    George, A.M.2
  • 26
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation
    • Kadaba N.S., Kaiser J.T., Johnson E., Lee A., and Rees D.C. The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321 (2008) 250-253
    • (2008) Science , vol.321 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 27
    • 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., and 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
  • 28
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D., Oldham M.L., Orelle C., Davidson A.L., and Chen J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell 33 (2009) 528-536
    • (2009) Mol. Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 29
    • 2342493863 scopus 로고    scopus 로고
    • Characterization of a nucleotide-binding domain associated with neisserial iron transport
    • Lau G.H., MacGillivray R.T., and Murphy M.E. Characterization of a nucleotide-binding domain associated with neisserial iron transport. J. Bacteriol. 186 (2004) 3266-3269
    • (2004) J. Bacteriol. , vol.186 , pp. 3266-3269
    • Lau, G.H.1    MacGillivray, R.T.2    Murphy, M.E.3
  • 31
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton K.J., and Higgins C.F. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28 (1998) 5-13
    • (1998) Mol. Microbiol. , vol.28 , pp. 5-13
    • Linton, K.J.1    Higgins, C.F.2
  • 32
    • 33846688359 scopus 로고    scopus 로고
    • Structure and function of ABC transporters: the ATP switch provides flexible control
    • Linton K.J., and Higgins C.F. Structure and function of ABC transporters: the ATP switch provides flexible control. Pflugers Arch. 453 (2007) 555-567
    • (2007) Pflugers Arch. , vol.453 , pp. 555-567
    • Linton, K.J.1    Higgins, C.F.2
  • 33
    • 29144502288 scopus 로고    scopus 로고
    • ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation
    • Lu G., Westbrooks J.M., Davidson A.L., and Chen J. ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation. Proc. Natl. Acad. Sci. USA 102 (2005) 17969-17974
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17969-17974
    • Lu, G.1    Westbrooks, J.M.2    Davidson, A.L.3    Chen, J.4
  • 34
    • 33748263407 scopus 로고    scopus 로고
    • Ergodic pumping: A mechanism to drive biomolecular conformation changes
    • MacKay R.S., and MacKay D.J.C. Ergodic pumping: A mechanism to drive biomolecular conformation changes. Physica D 216 (2006) 220-234
    • (2006) Physica D , vol.216 , pp. 220-234
    • MacKay, R.S.1    MacKay, D.J.C.2
  • 35
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • Minor W., Cymborowski M., Otwinowski Z., and Chruszcz M. HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes. Acta Crystallogr. D Biol. Crystallogr. 62 (2006) 859-866
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 36
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithm for rigid water molecules
    • Miyamoto S., and Kollman P.A. SETTLE: An analytical version of the SHAKE and RATTLE algorithm for rigid water molecules. J. Comput. Chem. 13 (1992) 952-962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 37
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • Moody J.E., Millen L., Binns D., Hunt J.F., and Thomas P.J. 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    Hunt, J.F.4    Thomas, P.J.5
  • 39
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham M.L., Khare D., Quiocho F.A., Davidson A.L., and Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450 (2007) 515-521
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 41
    • 33748776270 scopus 로고    scopus 로고
    • The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter
    • Oloo E.O., Fung E.Y., and Tieleman D.P. The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter. J. Biol. Chem. 281 (2006) 28397-28407
    • (2006) J. Biol. Chem. , vol.281 , pp. 28397-28407
    • Oloo, E.O.1    Fung, E.Y.2    Tieleman, D.P.3
  • 42
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink C., Villa A., Mark A.E., and van Gunsteren W.F. A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6. J. Comput. Chem. 25 (2004) 1656-1676
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    van Gunsteren, W.F.4
  • 45
    • 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., and Rees D.C. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315 (2007) 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
  • 47
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
    • Ryckaert J.-P., Ciccotti G., and Berendsen H.J.C. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comp. Phys. 23 (1977) 327-341
    • (1977) J. Comp. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 48
    • 33846794508 scopus 로고    scopus 로고
    • About a switch: how P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work
    • Sauna Z.E., and Ambudkar S.V. About a switch: how P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work. Mol. Cancer Ther. 6 (2007) 13-23
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 13-23
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 49
    • 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., and 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
  • 50
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41 (2005) 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 52
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger T.C. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 38-44
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 55
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward A., Reyes C.L., Yu J., Roth C.B., and Chang G. Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc. Natl. Acad. Sci. USA 104 (2007) 19005-19010
    • (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
  • 56
    • 58149359858 scopus 로고    scopus 로고
    • Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis
    • Wen P.C., and Tajkhorshid E. Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis. Biophys. J. 95 (2008) 5100-5110
    • (2008) Biophys. J. , vol.95 , pp. 5100-5110
    • Wen, P.C.1    Tajkhorshid, E.2
  • 57
    • 33748305808 scopus 로고    scopus 로고
    • A highly strained nuclear conformation of the exportin Cse1p revealed by molecular dynamics simulations
    • Zachariae U., and Grubmuller H. A highly strained nuclear conformation of the exportin Cse1p revealed by molecular dynamics simulations. Structure 14 (2006) 1469-1478
    • (2006) Structure , vol.14 , pp. 1469-1478
    • Zachariae, U.1    Grubmuller, H.2
  • 58
    • 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., and Schmitt L. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24 (2005) 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
  • 59
    • 27844467773 scopus 로고    scopus 로고
    • A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva J., Jenewein S., Oswald C., Jumpertz T., Holland I.B., and Schmitt L. A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB. Biochem. Soc. Trans. 33 (2005) 990-995
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 990-995
    • Zaitseva, J.1    Jenewein, S.2    Oswald, C.3    Jumpertz, T.4    Holland, I.B.5    Schmitt, L.6
  • 60
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer
    • Zaitseva J., Oswald C., Jumpertz T., Jenewein S., Wiedenmann A., Holland I.B., and Schmitt L. A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer. EMBO J. 25 (2006) 3432-3443
    • (2006) EMBO J. , vol.25 , pp. 3432-3443
    • Zaitseva, J.1    Oswald, C.2    Jumpertz, T.3    Jenewein, S.4    Wiedenmann, A.5    Holland, I.B.6    Schmitt, L.7


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