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Volumn 290, Issue 14, 2015, Pages 9135-9140

The allosteric regulatory mechanism of the escherichia coli metNI methionine ATP binding cassette (ABC) transporter

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BINDING SITES; ESCHERICHIA COLI; FEEDBACK; HYDROLYSIS; THERMOANALYSIS;

EID: 84926432107     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.603365     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 0015947712 scopus 로고
    • Transport systems for L-methionine in Escherichia coli
    • Kadner, R. J. (1974) Transport systems for L-methionine in Escherichia coli. J. Bacteriol. 117, 232-241
    • (1974) J. Bacteriol. , vol.117 , pp. 232-241
    • Kadner, R.J.1
  • 2
    • 0016232314 scopus 로고
    • Methionine transport in Escherichia coli: Physiological and genetic evidence for two uptake systems
    • Kadner, R. J., and Watson, W. J. (1974) Methionine transport in Escherichia coli: physiological and genetic evidence for two uptake systems. J. Bacteriol. 119, 401-409
    • (1974) J. Bacteriol. , vol.119 , pp. 401-409
    • Kadner, R.J.1    Watson, W.J.2
  • 3
    • 0016671558 scopus 로고
    • Regulation of methionine transport activity in Escherichia coli
    • Kadner, R. J. (1975) Regulation of methionine transport activity in Escherichia coli. J. Bacteriol. 122, 110-119
    • (1975) J. Bacteriol. , vol.122 , pp. 110-119
    • Kadner, R.J.1
  • 4
    • 0036776777 scopus 로고    scopus 로고
    • The Escherichia coli metD locus encodes an ABC transporter which includes Abc (MetN), YaeE (MetI), and YaeC (MetQ)
    • Merlin, C., Gardiner, G., Durand, S., and Masters, M. (2002) The Escherichia coli metD locus encodes an ABC transporter which includes Abc (MetN), YaeE (MetI), and YaeC (MetQ). J. Bacteriol. 184, 5513-5517
    • (2002) J. Bacteriol. , vol.184 , pp. 5513-5517
    • Merlin, C.1    Gardiner, G.2    Durand, S.3    Masters, M.4
  • 5
    • 0036720127 scopus 로고    scopus 로고
    • The metD D-methionine transporter locus of Escherichia coli is an ABC transporter gene cluster
    • Gál, J., Szvetnik, A., Schnell, R., and Kálmán, M. (2002) The metD D-methionine transporter locus of Escherichia coli is an ABC transporter gene cluster. J. Bacteriol. 184, 4930-4932
    • (2002) J. Bacteriol. , vol.184 , pp. 4930-4932
    • Gál, J.1    Szvetnik, A.2    Schnell, R.3    Kálmán, M.4
  • 6
    • 0041657693 scopus 로고    scopus 로고
    • A transporter of Escherichia coli specific for L- and D-methionine is the prototype for a new family within the ABC superfamily
    • Zhang, Z., Feige, J. N., Chang, A. B., Anderson, I. J., Brodianski, V. M., Vitreschak, A. G., Gelfand, M. S., and Saier, M. H., Jr. (2003) A transporter of Escherichia coli specific for L- and D-methionine is the prototype for a new family within the ABC superfamily. Arch. Microbiol. 180, 88-100
    • (2003) Arch. Microbiol. , vol.180 , pp. 88-100
    • Zhang, Z.1    Feige, J.N.2    Chang, A.B.3    Anderson, I.J.4    Brodianski, V.M.5    Vitreschak, A.G.6    Gelfand, M.S.7    Saier, M.H.8
  • 8
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J., and Locher, K. P. (2006) Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 9
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control inDNAdouble-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K. P., Karcher, A., Shin, D. S., Craig, L., Arthur, L. M., Carney, J. P., and Tainer, J. A. (2000) Structural biology of Rad50 ATPase: ATP-driven conformational control inDNAdouble-strand break repair and the ABC-ATPase superfamily. Cell 101, 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
  • 10
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from anABC 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 anABC 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
  • 11
    • 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. (2008) The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321, 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
  • 12
    • 84455200995 scopus 로고    scopus 로고
    • Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition
    • Johnson, E., Nguyen, P. T., Yeates, T. O., and Rees, D. C. (2012) Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition. Protein Sci. 21, 84-96
    • (2012) Protein Sci. , vol.21 , pp. 84-96
    • Johnson, E.1    Nguyen, P.T.2    Yeates, T.O.3    Rees, D.C.4
  • 13
    • 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. (2008) Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321, 246-250
    • (2008) Science , vol.321 , pp. 246-250
    • Gerber, S.1    Comellas-Bigler, M.2    Goetz, B.A.3    Locher, K.P.4
  • 14
    • 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. (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 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
  • 15
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. (1966) Simple allosteric model for membrane pumps. Nature 211, 969-970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 16
    • 84880511070 scopus 로고    scopus 로고
    • Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography
    • Chen, S., Oldham, M. L., Davidson, A. L., and Chen, J. (2013) Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography. Nature 499, 364-368
    • (2013) Nature , vol.499 , pp. 364-368
    • Chen, S.1    Oldham, M.L.2    Davidson, A.L.3    Chen, J.4
  • 17
    • 79957932347 scopus 로고    scopus 로고
    • Crystal structure of the maltose transporter in a pretranslocation intermediate state
    • Oldham, M. L., and Chen, J. (2011) Crystal structure of the maltose transporter in a pretranslocation intermediate state. Science 332, 1202-1205
    • (2011) Science , vol.332 , pp. 1202-1205
    • Oldham, M.L.1    Chen, J.2
  • 18
    • 84877012043 scopus 로고    scopus 로고
    • The maltose ABC transporter: Action of membrane lipids on the transporter stability, coupling and ATPase activity
    • Bao, H., Dalal, K., Wang, V., Rouiller, I., and Duong, F. (2013) The maltose ABC transporter: action of membrane lipids on the transporter stability, coupling and ATPase activity. Biochim. Biophys. Acta 1828, 1723-1730
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1723-1730
    • Bao, H.1    Dalal, K.2    Wang, V.3    Rouiller, I.4    Duong, F.5
  • 19
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson, A. L., Dassa, E., Orelle, C., and Chen, J. (2008) Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72, 317-364
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 20
    • 84867670628 scopus 로고    scopus 로고
    • Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F
    • Korkhov, V. M., Mireku, S. A., and Locher, K. P. (2012) Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F. Nature 490, 367-372
    • (2012) Nature , vol.490 , pp. 367-372
    • Korkhov, V.M.1    Mireku, S.A.2    Locher, K.P.3
  • 21
    • 84875833653 scopus 로고    scopus 로고
    • A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization
    • Tal, N., Ovcharenko, E., and Lewinson, O. (2013) A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization. Proc. Natl. Acad. Sci. U.S.A. 110, 5434-5439
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 5434-5439
    • Tal, N.1    Ovcharenko, E.2    Lewinson, O.3
  • 22
    • 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
  • 23
    • 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
    • 68049100110 scopus 로고    scopus 로고
    • Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli
    • Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., and Rabinowitz, J. D. (2009) Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. Nat. Chem. Biol. 5, 593-599
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 593-599
    • Bennett, B.D.1    Kimball, E.H.2    Gao, M.3    Osterhout, R.4    Van Dien, S.J.5    Rabinowitz, J.D.6
  • 26
    • 84894446749 scopus 로고    scopus 로고
    • Determination of parameter identifiability in nonlinear biophysical models: A Bayesian approach
    • Hines, K. E., Middendorf, T. R., and Aldrich, R. W. (2014) Determination of parameter identifiability in nonlinear biophysical models: a Bayesian approach. J. Gen. Physiol. 143, 401-416
    • (2014) J. Gen. Physiol. , vol.143 , pp. 401-416
    • Hines, K.E.1    Middendorf, T.R.2    Aldrich, R.W.3
  • 27
    • 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., and Davidson, A. L. (2001) Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport. Proc. Natl. Acad. Sci. U.S.A. 98, 1525-1530
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 28
    • 84923799962 scopus 로고    scopus 로고
    • Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F
    • Korkhov, V. M., Mireku, S. A., Veprintsev, D. B., and Locher, K. P. (2014) Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F. Nat. Struct. Mol. Biol. 21, 1097-1099
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 1097-1099
    • Korkhov, V.M.1    Mireku, S.A.2    Veprintsev, D.B.3    Locher, K.P.4
  • 29
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher, J., Francke, C., and Postma, P. W. (2006) How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol. Mol. Biol. Rev. 70, 939-1031
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 30
    • 84882324018 scopus 로고    scopus 로고
    • Phosphatidylglycerol directs binding and inhibitory action of EIIAGlc protein on the maltose transporter
    • Bao, H., and Duong, F. (2013) Phosphatidylglycerol directs binding and inhibitory action of EIIAGlc protein on the maltose transporter. J. Biol. Chem. 288, 23666-23674
    • (2013) J. Biol. Chem. , vol.288 , pp. 23666-23674
    • Bao, H.1    Duong, F.2
  • 31
    • 0345074107 scopus 로고    scopus 로고
    • Osmoregulation in Lactococcus lactis: BusR, a transcriptional repressor of the glycine betaine uptake system BusA
    • Romeo, Y., Obis, D., Bouvier, J., Guillot, A., Fourçans, A., Bouvier, I., Gutierrez, C., and Mistou, M. Y. (2003) Osmoregulation in Lactococcus lactis: BusR, a transcriptional repressor of the glycine betaine uptake system BusA. Mol. Microbiol. 47, 1135-1147
    • (2003) Mol. Microbiol. , vol.47 , pp. 1135-1147
    • Romeo, Y.1    Obis, D.2    Bouvier, J.3    Guillot, A.4    Fourçans, A.5    Bouvier, I.6    Gutierrez, C.7    Mistou, M.Y.8
  • 32
    • 0035910510 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator Cl- channels with R domain deletions and translocations show phosphorylation-dependent and -independent activity
    • Baldursson, O., Ostedgaard, L. S., Rokhlina, T., Cotten, J. F., and Welsh, M. J. (2001) Cystic fibrosis transmembrane conductance regulator Cl- channels with R domain deletions and translocations show phosphorylation-dependent and -independent activity. J. Biol. Chem. 276, 1904-1910
    • (2001) J. Biol. Chem. , vol.276 , pp. 1904-1910
    • Baldursson, O.1    Ostedgaard, L.S.2    Rokhlina, T.3    Cotten, J.F.4    Welsh, M.J.5
  • 33
    • 23844483240 scopus 로고    scopus 로고
    • Phosphorylation of CFTR by PKA promotes binding of the regulatory domain
    • Chappe, V., Irvine, T., Liao, J., Evagelidis, A., and Hanrahan, J. W. (2005) Phosphorylation of CFTR by PKA promotes binding of the regulatory domain. EMBO J. 24, 2730-2740
    • (2005) EMBO J. , vol.24 , pp. 2730-2740
    • Chappe, V.1    Irvine, T.2    Liao, J.3    Evagelidis, A.4    Hanrahan, J.W.5
  • 34
    • 0033817333 scopus 로고    scopus 로고
    • Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains
    • Csanády, L., Chan, K. W., Seto-Young, D., Kopsco, D. C., Nairn, A. C., and Gadsby, D. C. (2000) Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains. J. Gen. Physiol. 116, 477-500
    • (2000) J. Gen. Physiol. , vol.116 , pp. 477-500
    • Csanády, L.1    Chan, K.W.2    Seto-Young, D.3    Kopsco, D.C.4    Nairn, A.C.5    Gadsby, D.C.6
  • 35
    • 0027171978 scopus 로고
    • Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by negative charge in the R domain
    • Rich, D. P., Berger, H. A., Cheng, S. H., Travis, S. M., Saxena, M., Smith, A. E., and Welsh, M. J. (1993) Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by negative charge in the R domain. J. Biol. Chem. 268, 20259-20267
    • (1993) J. Biol. Chem. , vol.268 , pp. 20259-20267
    • Rich, D.P.1    Berger, H.A.2    Cheng, S.H.3    Travis, S.M.4    Saxena, M.5    Smith, A.E.6    Welsh, M.J.7


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