메뉴 건너뛰기




Volumn 44, Issue 28, 2005, Pages 9680-9690

Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CELL MEMBRANES; HYDROLYSIS; MOLECULAR BIOLOGY; OLIGOMERS; PROTEINS;

EID: 22244452024     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0506122     Document Type: Article
Times cited : (86)

References (59)
  • 1
    • 85163467886 scopus 로고    scopus 로고
    • Bacterial ABC transporters involved in protein translocationin
    • (Holland, I. B., Cole, S. P. C, Kuchler, K., and Higgins, C. F., Eds.), Academic Press (Elsevier Science), London
    • Holland, I. B., Benabdelhak, H., Young, J., Pimenta, A. L., Schmitt, L., and Blight, M. (2003) Bacterial ABC transporters involved in protein translocationin, in ABC Proteins: From Bacteria to Man (Holland, I. B., Cole, S. P. C, Kuchler, K., and Higgins, C. F., Eds.) pp 209-241, Academic Press (Elsevier Science), London.
    • (2003) ABC Proteins: From Bacteria to Man , pp. 209-241
    • Holland, I.B.1    Benabdelhak, H.2    Young, J.3    Pimenta, A.L.4    Schmitt, L.5    Blight, M.6
  • 2
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis, V., Sharff, A., Koronakis, E., Luisi, B., and Hughes, C. (2000) Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export, Nature 405, 914-919
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 3
    • 0033020320 scopus 로고    scopus 로고
    • Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator
    • Pimenta, A. L., Young, J., Holland, I. B., and Blight, M. A. (1999) Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator, Mol. Gen. Genet. 261, 122-132.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 122-132
    • Pimenta, A.L.1    Young, J.2    Holland, I.B.3    Blight, M.A.4
  • 5
    • 0027551081 scopus 로고
    • Bacterial signal peptide-independent protein export: HlyB-directed secretion of hemolysin
    • Koronakis, V., and Hughes, C. (1993) Bacterial signal peptide-independent protein export: HlyB-directed secretion of hemolysin, Semin. Cell Biol. 4, 1-15.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 1-15
    • Koronakis, V.1    Hughes, C.2
  • 6
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman, M. M., and Pastan, I. (1993) Biochemistry of multidrug resistance mediated by the multidrug transporter, Annu. Rev. Biochem. 62, 385-427.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 7
    • 0034601092 scopus 로고    scopus 로고
    • Affinity, specificity, diversity: A challenge for the ABC transporter TAP in cellular immunity
    • Schmitt, L., and Tampe, R. (2000) Affinity, specificity, diversity: a challenge for the ABC transporter TAP in cellular immunity, ChemBioChem 1, 16-35.
    • (2000) ChemBioChem , vol.1 , pp. 16-35
    • Schmitt, L.1    Tampe, R.2
  • 8
    • 0035004765 scopus 로고    scopus 로고
    • Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease
    • Ames, G. F., Nikaido, K., Wang, I. X., Liu, P. Q., Liu, C. E., and Hu, C. (2001) Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease, J. Bioenerg. Biomembr. 33, 79-92.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 79-92
    • Ames, G.F.1    Nikaido, K.2    Wang, I.X.3    Liu, P.Q.4    Liu, C.E.5    Hu, C.6
  • 9
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland, I. B., and Blight, M. A. (1999) ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans, J. Mol. Biol. 293, 381-399.
    • (1999) J. Mol. Biol. , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 10
    • 0029955151 scopus 로고    scopus 로고
    • The proteins encoded by the rbs operon of Escherichia coli: I. Overproduction, purification, characterization, and functional analysis of RbsA
    • Barroga, C. F., Zhang, H., Wajih, N., Bouyer, J. H., and Hermodson, M. A. (1996) The proteins encoded by the rbs operon of Escherichia coli: I. Overproduction, purification, characterization, and functional analysis of RbsA, Protein Sci. 5, 1093-1099.
    • (1996) Protein Sci. , vol.5 , pp. 1093-1099
    • Barroga, C.F.1    Zhang, H.2    Wajih, N.3    Bouyer, J.H.4    Hermodson, M.A.5
  • 11
    • 0037055994 scopus 로고    scopus 로고
    • Multidrug transporters and antibiotic resistance in Lactococcus lactis
    • Poelarends, G. J., Mazurkiewicz, P., and Konings, W. N. (2002) Multidrug transporters and antibiotic resistance in Lactococcus lactis, Biochim. Biophys. Acta 1555, 1-7.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 1-7
    • Poelarends, G.J.1    Mazurkiewicz, P.2    Konings, W.N.3
  • 12
    • 0036909285 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Schmitt, L., and Tampe, R. (2002) Structure and mechanism of ABC transporters, Curr. Opin. Struct. Biol. 12, 754-760.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 754-760
    • Schmitt, L.1    Tampe, R.2
  • 13
    • 21244474713 scopus 로고    scopus 로고
    • Analysis of the properties of the isolated ABC-ATPase domain of HlyB: Activity shows positive co-operativity but dimers appear highly unstable
    • Benabdelhak, H., Schmitt, L., Horn, C., Kiontke, S., Jumel, K., Blight, M. A., and Holland, I. B. (2005) Analysis of the properties of the isolated ABC-ATPase domain of HlyB: activity shows positive co-operativity but dimers appear highly unstable, Biochem. J. 368, 1-7.
    • (2005) Biochem. J. , vol.368 , pp. 1-7
    • Benabdelhak, H.1    Schmitt, L.2    Horn, C.3    Kiontke, S.4    Jumel, K.5    Blight, M.A.6    Holland, I.B.7
  • 14
    • 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., and Stubbs, M. T. (2003) 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) 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
  • 15
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A. L., and 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
  • 16
    • 0037133735 scopus 로고    scopus 로고
    • Structure and association of ATP-binding cassette transporter nucleotide-binding domains
    • Kerr, I. D. (2002) Structure and association of ATP-binding cassette transporter nucleotide-binding domains, Biochim. Biophys. Acta 1561, 47-64.
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 47-64
    • Kerr, I.D.1
  • 17
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter
    • Guzman, L.-M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter, J. Bacteriol. 177, 4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.-M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 18
    • 16644362409 scopus 로고    scopus 로고
    • The role of CAPS buffer in expanding the crystallization space of the nucleotide-binding domain of the ABC transporter haemolysin B from Escherichia coli
    • Zaitseva, J., Holland, I. B., and Schmitt, L. (2004) The role of CAPS buffer in expanding the crystallization space of the nucleotide-binding domain of the ABC transporter haemolysin B from Escherichia coli, Acta Crystallogr., Sect. D 60, 1076-1084.
    • (2004) Acta Crystallogr., Sect. D , vol.60 , pp. 1076-1084
    • Zaitseva, J.1    Holland, I.B.2    Schmitt, L.3
  • 19
    • 0030011312 scopus 로고    scopus 로고
    • The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC
    • Zaitseva, J., Zhang, H., Binnie, R. A., and Hermodson, M. (1996) The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC, Protein Sci. 5, 1100-1107.
    • (1996) Protein Sci. , vol.5 , pp. 1100-1107
    • Zaitseva, J.1    Zhang, H.2    Binnie, R.A.3    Hermodson, M.4
  • 20
    • 0023917654 scopus 로고
    • A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay
    • Baykov, A. A., Evtushenko, O. A., and Avaeva, S. M. (1988) A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay, Anal. Biochem. 171, 266-270.
    • (1988) Anal. Biochem. , vol.171 , pp. 266-270
    • Baykov, A.A.1    Evtushenko, O.A.2    Avaeva, S.M.3
  • 21
    • 0024964932 scopus 로고
    • Competitive binding of ATP and the fluorescent substrate analogue 2′,3′-O-(2,4,6-trinitrophenylcyclohexadienylidine) adenosine 5′-triphosphate to the gastric H+, K+-ATPase: Evidence for two classes of nucleotide sites
    • Faller, L. D. (1989) Competitive binding of ATP and the fluorescent substrate analogue 2′,3′-O-(2,4,6- trinitrophenylcyclohexadienylidine) adenosine 5′-triphosphate to the gastric H+, K+-ATPase: evidence for two classes of nucleotide sites, Biochemistry 25, 6771-6778.
    • (1989) Biochemistry , vol.25 , pp. 6771-6778
    • Faller, L.D.1
  • 22
    • 0030822352 scopus 로고    scopus 로고
    • Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity
    • Nikaido, K., Liu, P. Q., and Ames, G. F. (1997) Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity, J. Biol. Chem. 272, 27745-27752.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27745-27752
    • Nikaido, K.1    Liu, P.Q.2    Ames, G.F.3
  • 23
    • 0038711772 scopus 로고    scopus 로고
    • The ATP hydrolysis cycle of the nucleotide-binding domain of the mitocnondrial ATP-binding cassette transporter Md11p
    • Janas, E., Hofacker, M., Chen, M., Gompf, S., van der Does, C., and Tampe, R. (2003) The ATP hydrolysis cycle of the nucleotide-binding domain of the mitocnondrial ATP-binding cassette transporter Md11p, J. Biol. Chem. 278, 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
  • 24
    • 0030803791 scopus 로고    scopus 로고
    • Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter)
    • Liu, C. E., Liu, P. Q., and Ames, G. F. (1997) Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter), J. Biol. Chem. 272, 21883-21891.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21883-21891
    • Liu, C.E.1    Liu, P.Q.2    Ames, G.F.3
  • 25
    • 0028362501 scopus 로고
    • Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch, I. L., Al-Shawei, M. K., and Senior, A. E. (1994) Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein, Biochemistry 33, 7069-7076.
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Urbatsch, I.L.1    Al-Shawei, M.K.2    Senior, A.E.3
  • 26
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP-hydrolysis in the nucleotide binding doamin of the ABC-transporter HlyB
    • Zaitseva, J., Jenewein, S., Jumpertz, T., Holland, I. B., and Schmitt, L. (2005) H662 is the linchpin of ATP-hydrolysis in the nucleotide binding doamin 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
  • 27
    • 0031019498 scopus 로고    scopus 로고
    • Stabilization of ion selectivity filter by pore loop ion pairs in an inwardly rectifying potassium channel
    • Yang, J., Yu, M., Jan, Y. N., and Jan, L. Y. (1997) Stabilization of ion selectivity filter by pore loop ion pairs in an inwardly rectifying potassium channel, Proc. Natl. Acad. Sci. U.S A. 94, 1568-1572.
    • (1997) Proc. Natl. Acad. Sci. U.S A. , vol.94 , pp. 1568-1572
    • Yang, J.1    Yu, M.2    Jan, Y.N.3    Jan, L.Y.4
  • 28
    • 0033957143 scopus 로고    scopus 로고
    • Substrate-assisted catalysis: Molecular basis and biological significance
    • Dall'Acqua, W., and Carter, P. (2000) Substrate-assisted catalysis: molecular basis and biological significance, Protein Sci. 9, 1-9.
    • (2000) Protein Sci. , vol.9 , pp. 1-9
    • Dall'Acqua, W.1    Carter, P.2
  • 29
    • 0032421666 scopus 로고    scopus 로고
    • Relevance of divalent cations to ATP-driven proton pumping in beef heart mitochondrial F0F1-ATPase
    • Papageorgiou, S., Melandri, A. B., and Solaini, G. (1998) Relevance of divalent cations to ATP-driven proton pumping in beef heart mitochondrial F0F1-ATPase, J. Bioenerg. Biomembr. 30, 533-541.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 533-541
    • Papageorgiou, S.1    Melandri, A.B.2    Solaini, G.3
  • 31
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch, I. L., Sankaran, B., Weber, J., and Senior, A. E. (1995) P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site, J. Biol. Chem. 270, 19383-19390.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 32
    • 0242494861 scopus 로고    scopus 로고
    • Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis
    • Horn, C., Bremer, E., and Schmitt, L. (2003) Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis, J. Mol. Biol. 334, 403-419.
    • (2003) J. Mol. Biol. , vol.334 , pp. 403-419
    • Horn, C.1    Bremer, E.2    Schmitt, L.3
  • 33
    • 0030689692 scopus 로고    scopus 로고
    • ATPase activity of purified multidrug resistance-associated protein
    • Chang, X. B., Hou, Y. X., and Riordan, J. R. (1997) ATPase activity of purified multidrug resistance-associated protein, J. Biol. Chem. 272, 30962-30968.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30962-30968
    • Chang, X.B.1    Hou, Y.X.2    Riordan, J.R.3
  • 35
    • 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. (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
  • 36
    • 0035955547 scopus 로고    scopus 로고
    • Substrate-triggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli
    • Balakrishnan, L., Hughes, C., and Koronakis, V. (2001) Substrate-triggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli, J. Mol. Biol. 313, 501-510.
    • (2001) J. Mol. Biol. , vol.313 , pp. 501-510
    • Balakrishnan, L.1    Hughes, C.2    Koronakis, V.3
  • 37
    • 0030696854 scopus 로고    scopus 로고
    • In vivo and in vitro studies on interactions between the components of the hemolysin (HlyA) secretion machinery of Escherichia coli
    • Schlor, S., Schmidt, A., Maier, E., Benz, R., Goebel, W., and Gentschev, I. (1997) In vivo and in vitro studies on interactions between the components of the hemolysin (HlyA) secretion machinery of Escherichia coli, Mol. Gen. Genet. 256, 306-319.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 306-319
    • Schlor, S.1    Schmidt, A.2    Maier, E.3    Benz, R.4    Goebel, W.5    Gentschev, I.6
  • 38
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E.coli: Reversible bridging of an inner-membrane translocase to an outer membrane exit pore
    • Thanabalu, T., Koronakis, E., Hughes, C., and Koronakis, V. (1998) Substrate-induced assembly of a contiguous channel for protein export from E.coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore, EMBO J. 17, 6487-6496.
    • (1998) EMBO J. , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 39
    • 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. (2002) Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters, J. Biol. Chem. 277, 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
  • 40
    • 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. (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
  • 41
    • 0242321011 scopus 로고    scopus 로고
    • Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus
    • Verdon, G., Albers, S. V., van Oosterwijk, N., Dijkstra, B. W., Driessen, A. J., and Thunnissen, A. M. (2003) Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus, J. Mol. Biol. 334, 255-267.
    • (2003) J. Mol. Biol. , vol.334 , pp. 255-267
    • Verdon, G.1    Albers, S.V.2    Van Oosterwijk, N.3    Dijkstra, B.W.4    Driessen, A.J.5    Thunnissen, A.M.6
  • 42
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L. W., Wang, I. X., Nikaido, K., Liu, P. Q., Ames, G. F., and 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.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.5    Kim, S.H.6
  • 43
    • 0035801375 scopus 로고    scopus 로고
    • Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing
    • Gaudet, R., and Wiley, D. C. (2001) Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing, EMBO J. 20, 4964-4972.
    • (2001) EMBO J. , vol.20 , pp. 4964-4972
    • Gaudet, R.1    Wiley, D.C.2
  • 44
    • 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. (2001) 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) 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
  • 45
    • 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., and Hunt, J. F. (2001) 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, 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
  • 46
    • 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., and Thunnissen, A. M. (2003) Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations, J. Mol. Biol. 330, 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.4    Thunnissen, A.M.5
  • 48
    • 0347356332 scopus 로고    scopus 로고
    • Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: Evidence for interaction between ATP and Trp653
    • Ramaen, O., Masscheleyn, S., Duffieux, F., Pamlard, O., Oberkampf, M., Lallemand, J. Y., Stoven, V., and Jacquet, E. (2003) Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653, Biochem. J. 376, 749-756.
    • (2003) Biochem. J. , vol.376 , pp. 749-756
    • Ramaen, O.1    Masscheleyn, S.2    Duffieux, F.3    Pamlard, O.4    Oberkampf, M.5    Lallemand, J.Y.6    Stoven, V.7    Jacquet, E.8
  • 49
    • 0020361477 scopus 로고
    • Stoichiometry of the H+-ATPase of growing and resting, aerobic Escherichia coli
    • Kashket, E. R. (1982) Stoichiometry of the H+-ATPase of growing and resting, aerobic Escherichia coli, Biochemistry 21, 5534-5538.
    • (1982) Biochemistry , vol.21 , pp. 5534-5538
    • Kashket, E.R.1
  • 50
    • 0042818091 scopus 로고    scopus 로고
    • Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex
    • Samanta, S., Ayvaz, T., Reyes, M., Shuman, H. A., Chen, J., and Davidson, A. L. (2003) Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex, J. Biol. Chem. 275, 35265-35271.
    • (2003) J. Biol. Chem. , vol.275 , pp. 35265-35271
    • Samanta, S.1    Ayvaz, T.2    Reyes, M.3    Shuman, H.A.4    Chen, J.5    Davidson, A.L.6
  • 51
    • 0033575309 scopus 로고    scopus 로고
    • Molecular and biochemical analysis of MalK, the ATP-hydrolyzing subunit of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis
    • Greller, G., Horlacher, R., DiRuggiero, J., and Boos, W. (1999) Molecular and biochemical analysis of MalK, the ATP-hydrolyzing subunit of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis, J. Biol. Chem. 274, 20259-20264.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20259-20264
    • Greller, G.1    Horlacher, R.2    DiRuggiero, J.3    Boos, W.4
  • 52
    • 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. (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
  • 53
    • 0037162468 scopus 로고    scopus 로고
    • Vanadate-catalyzed photocleavage of the signature motif of an ATP-binding cassette (ABC) transporter
    • Fetsch, E. E., and Davidson, A. L. (2002) Vanadate-catalyzed photocleavage of the signature motif of an ATP-binding cassette (ABC) transporter, Proc. Natl. Acad. Sci. U.S.A. 99, 9685-9690.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 9685-9690
    • Fetsch, E.E.1    Davidson, A.L.2
  • 54
    • 8744266443 scopus 로고    scopus 로고
    • Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues
    • Tombline, G., Bartholomew, L. A., Tyndall, G. A., Gimi, K., Urbatsch, I. L., and Senior, A. E. (2004) Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues, J. Biol. Chem. 279, 46518-46526.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46518-46526
    • Tombline, G.1    Bartholomew, L.A.2    Tyndall, G.A.3    Gimi, K.4    Urbatsch, I.L.5    Senior, A.E.6
  • 55
    • 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., and Ames, G. F. (1999) 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) J. Biol. Chem. , vol.274 , pp. 26727-26735
    • Nikaido, K.1    Ames, G.F.2
  • 56
    • 0025954269 scopus 로고
    • Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations
    • Shyamala, V., Baichwal, V., Beall, E., and Ames, G. F. (1991) Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations, J. Biol. Chem. 266, 18714-18719.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18714-18719
    • Shyamala, V.1    Baichwal, V.2    Beall, E.3    Ames, G.F.4
  • 57
    • 0030886132 scopus 로고    scopus 로고
    • Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli
    • Davidson, A. L., and Sharma, S. (1997) Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli, J. Bacteriol. 179, 5458-5464.
    • (1997) J. Bacteriol. , vol.179 , pp. 5458-5464
    • Davidson, A.L.1    Sharma, S.2
  • 58
    • 0027126818 scopus 로고
    • Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family
    • Walter, C., Wilken, S., and Schneider, E. (1992) Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family [corrected], FEBS Lett. 303, 41-44.
    • (1992) FEBS Lett. , vol.303 , pp. 41-44
    • Walter, C.1    Wilken, S.2    Schneider, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.