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Volumn 20, Issue 11, 2013, Pages 1310-1317

Structural insights into H +-coupled multidrug extrusion by a MATE transporter

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; DNA DAMAGE INDUCIBLE PROTEIN F; HYDROGEN; MULTIDRUG AND TOXIC COMPOUND EXTRUSION TRANSPORTER; PEPTIDES AND PROTEINS; SODIUM ION; UNCLASSIFIED DRUG;

EID: 84887491471     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2687     Document Type: Article
Times cited : (83)

References (40)
  • 1
    • 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
  • 2
    • 69549111337 scopus 로고    scopus 로고
    • Antibiotics for emerging pathogens
    • Fischbach, M.A. & Walsh, C.T. Antibiotics for emerging pathogens. Science 325, 1089-1093 (2009).
    • (2009) Science , vol.325 , pp. 1089-1093
    • Fischbach, M.A.1    Walsh, C.T.2
  • 3
    • 0032949426 scopus 로고    scopus 로고
    • The multidrug efflux protein NorM is a prototype of a new family of transporters
    • Brown, M.H., Paulsen, I.T. & Skurray, R.A. The multidrug efflux protein NorM is a prototype of a new family of transporters. Mol. Microbiol. 31, 394-395 (1999).
    • (1999) Mol. Microbiol. , vol.31 , pp. 394-395
    • Brown, M.H.1    Paulsen, I.T.2    Skurray, R.A.3
  • 4
    • 33749988040 scopus 로고    scopus 로고
    • The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations
    • Omote, H., Miasa, M., Matsumoto, T., Otsuka, M. & Moroyama, Y. The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations. Trends Pharmacol. Sci. 27, 587-593 (2006).
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 587-593
    • Omote, H.1    Miasa, M.2    Matsumoto, T.3    Otsuka, M.4    Moroyama, Y.5
  • 5
    • 64649085938 scopus 로고    scopus 로고
    • Multidrug efflux transporters in the MATE family
    • Kuroda, T. & Tsuchiya, T. Multidrug efflux transporters in the MATE family. Biochim. Biophys. Acta 1794, 763-768 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 763-768
    • Kuroda, T.1    Tsuchiya, T.2
  • 6
    • 0034459552 scopus 로고    scopus 로고
    • NorM of Vibrio parahaemolyticus is an Na+-driven multidrug efflux pump
    • Morita, Y., Kataoka, A., Shiota, S., Mizushima, T. & Tsuchiya, T. NorM of Vibrio parahaemolyticus is an Na+-driven multidrug efflux pump. J. Bacteriol. 182, 6694-6697 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 6694-6697
    • Morita, Y.1    Kataoka, A.2    Shiota, S.3    Mizushima, T.4    Tsuchiya, T.5
  • 7
    • 0036134936 scopus 로고    scopus 로고
    • VmrA, a member of a novel class of Na+-coupled multidrug efflux pumps from Vibrio parahaemolyticus
    • Chen, J. et al. VmrA, a member of a novel class of Na+-coupled multidrug efflux pumps from Vibrio parahaemolyticus. J. Bacteriol. 184, 572-576 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 572-576
    • Chen, J.1
  • 8
    • 50949102768 scopus 로고    scopus 로고
    • Functional cloning and characterization of the multidrug efflux pumps NorM from Neisseria gonorrhoeae and YdhE from Escherichia coli
    • Long, F., Rouquette-Loughlin, C., Shafer, W.M. & Yu, E.W. Functional cloning and characterization of the multidrug efflux pumps NorM from Neisseria gonorrhoeae and YdhE from Escherichia coli. Antimicrob. Agents Chemother. 52, 3052-3060 (2008).
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 3052-3060
    • Long, F.1    Rouquette-Loughlin, C.2    Shafer, W.M.3    Yu, E.W.4
  • 9
    • 0346991732 scopus 로고    scopus 로고
    • An H+-coupled multidrug efflux pump, PmpM, a member of the MATE family of transporters, from Pseudomonas aeruginosa
    • Hr, G.X. et al. An H+-coupled multidrug efflux pump, PmpM, a member of the MATE family of transporters, from Pseudomonas aeruginosa. J. Bacteriol. 186, 262-265 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 262-265
    • Hr, G.X.1
  • 10
    • 25844455664 scopus 로고    scopus 로고
    • AbeM an H+-coupled Acinetobacter baumannii multidrug efflux pump belonging to the MATE family of transporters
    • Su, X.Z., Chen, J., Mizushima, T., Kuroda, T. & Tsuchiya, T. AbeM, an H+-coupled Acinetobacter baumannii multidrug efflux pump belonging to the MATE family of transporters. Antimicrob. Agents Chemother. 49, 4362-4364 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4362-4364
    • Su, X.Z.1    Chen, J.2    Mizushima, T.3    Kuroda, T.4    Tsuchiya, T.5
  • 11
    • 0037085468 scopus 로고    scopus 로고
    • Functional cloning and characterization of a plant efflux carrier for multidrug and heavy metal detoxification
    • Li, L., He, Z., Pandey, G.K., Tsuchiya, T. & Luan, S. Functional cloning and characterization of a plant efflux carrier for multidrug and heavy metal detoxification. J. Biol. Chem. 277, 5360-5368 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 5360-5368
    • Li, L.1    He, Z.2    Pandey, G.K.3    Tsuchiya, T.4    Luan, S.5
  • 12
    • 29144523534 scopus 로고    scopus 로고
    • A human transporter protein that mediates the final excretion step for toxic organic cations
    • Otsuka, M. et al. A human transporter protein that mediates the final excretion step for toxic organic cations. Proc. Natl. Acad. Sci. USA 102, 17923-17928 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17923-17928
    • Otsuka, M.1
  • 13
    • 33746548445 scopus 로고    scopus 로고
    • Identification and functional characterization of a new human kidney-specific H+/organic cation antiporter, kidney-specific multidrug and toxin extrusion 2
    • Masuda, S. et al. Identification and functional characterization of a new human kidney-specific H+/organic cation antiporter, kidney-specific multidrug and toxin extrusion 2. J. Am. Soc. Nephrol. 17, 2127-2135 (2006).
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 2127-2135
    • Masuda, S.1
  • 14
    • 77958596325 scopus 로고    scopus 로고
    • Structure of a cation-bound multidrug and toxic compound extrusion transporter
    • He, X. et al. Structure of a cation-bound multidrug and toxic compound extrusion transporter. Nature 467, 991-994 (2010).
    • (2010) Nature , vol.467 , pp. 991-994
    • He, X.1
  • 15
    • 84873431135 scopus 로고    scopus 로고
    • Structures of a Na+-coupled, substrate-bound MATE multidrug transporter
    • Lu, M. et al. Structures of a Na+-coupled, substrate-bound MATE multidrug transporter. Proc. Natl. Acad. Sci. USA 110, 2099-2104 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 2099-2104
    • Lu, M.1
  • 16
    • 0001398337 scopus 로고
    • A general theory of membrane transport from studies of bacteria
    • Mitchell, P. A general theory of membrane transport from studies of bacteria. Nature 180, 134-136 (1957).
    • (1957) Nature , vol.180 , pp. 134-136
    • Mitchell, P.1
  • 17
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. Simple allosteric model for membrane pumps. Nature 211, 969-970 (1966).
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 18
    • 0038647631 scopus 로고    scopus 로고
    • Gene cloning and characterization of VcrM, a Na+-coupled multidrug efflux pump, from Vibrio cholerae non-O1
    • Huda, M.N. et al. Gene cloning and characterization of VcrM, a Na+-coupled multidrug efflux pump, from Vibrio cholerae non-O1. Microbiol. Immunol. 47, 419-427 (2003).
    • (2003) Microbiol. Immunol. , vol.47 , pp. 419-427
    • Huda, M.N.1
  • 19
    • 4644306334 scopus 로고    scopus 로고
    • CdeA of Clostridium difficile, a new multidrug efflux transporter of the MATE family
    • Dridi, L., Tankoviv, J. & Petit, J.C. CdeA of Clostridium difficile, a new multidrug efflux transporter of the MATE family. Microb. Drug Resist. 10, 191-196 (2004).
    • (2004) Microb. Drug Resist. , vol.10 , pp. 191-196
    • Dridi, L.1    Tankoviv, J.2    Petit, J.C.3
  • 20
    • 34248143835 scopus 로고    scopus 로고
    • The host-induced Ralstonia solanacearum genes, acrA and dinF, encode multidrug efflux pumps and contribute to bacterial wilt virulence
    • Brown, D.G., Swanson, J.K. & Allen, C. The host-induced Ralstonia solanacearum genes, acrA and dinF, encode multidrug efflux pumps and contribute to bacterial wilt virulence. Appl. Environ. Microbiol. 73, 2777-2786 (2007).
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 2777-2786
    • Brown, D.G.1    Swanson, J.K.2    Allen, C.3
  • 22
    • 14244266607 scopus 로고    scopus 로고
    • Identification of essential amino acid residues of the NorM Na+/multidrug antiporter in Vibrio parahaemolyticus
    • Otsuka, M. et al. Identification of essential amino acid residues of the NorM Na+/multidrug antiporter in Vibrio parahaemolyticus. J. Bacteriol. 187, 1552-1558 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 1552-1558
    • Otsuka, M.1
  • 23
    • 41949103043 scopus 로고    scopus 로고
    • Role of glutamate residues in substrate recognition by human MATE1 polyspecific H+/organic cation exporter
    • Matsumoto, T., Kanamoto, T., Otsuka, M., Omote, H. & Moriyama, Y. Role of glutamate residues in substrate recognition by human MATE1 polyspecific H+/organic cation exporter. Am. J. Physiol. Cell Physiol. 294, C1074-C1078 (2008).
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294
    • Matsumoto, T.1    Kanamoto, T.2    Otsuka, M.3    Omote, H.4    Moriyama, Y.5
  • 24
    • 33746016294 scopus 로고    scopus 로고
    • Potassium/proton antiporter system of Escherichia coli
    • Radchenko, M.V. et al. Potassium/proton antiporter system of Escherichia coli. J. Biol. Chem. 281, 19822-19829 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 19822-19829
    • Radchenko, M.V.1
  • 25
    • 84866280173 scopus 로고    scopus 로고
    • Dissection of mechanistic principles of a secondary multidrug efflux protein
    • Fluman, N., Ryan, C.M., Whitelegge, J.P. & Bibi, E. Dissection of mechanistic principles of a secondary multidrug efflux protein. Mol. Cell 47, 777-787 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 777-787
    • Fluman, N.1    Ryan, C.M.2    Whitelegge, J.P.3    Bibi, E.4
  • 26
    • 37649009221 scopus 로고    scopus 로고
    • X-ray structure of EmrE supports dual topology model
    • Chen, Y.J. et al. X-ray structure of EmrE supports dual topology model. Proc. Natl. Acad. Sci. USA 104, 18999-19004 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18999-19004
    • Chen, Y.J.1
  • 27
    • 57349090665 scopus 로고    scopus 로고
    • Very fast prediction and rationalization of pKa values for protein-ligand complexes
    • Bas, D.C., Rogers, D.M. & Jensen, J.H. Very fast prediction and rationalization of pKa values for protein-ligand complexes. Proteins 73, 765-783 (2008).
    • (2008) Proteins , vol.73 , pp. 765-783
    • Bas, D.C.1    Rogers, D.M.2    Jensen, J.H.3
  • 28
    • 36749095723 scopus 로고    scopus 로고
    • The fast release of sticky protons: Kinetics of substrate binding and proton release in a multidrug transporter
    • Adam, Y., Tayer, N., Rotem, D., Schteiber, G. & Schudiner, S. The fast release of sticky protons: kinetics of substrate binding and proton release in a multidrug transporter. Proc. Natl. Acad. Sci. USA 104, 17989-17994 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17989-17994
    • Adam, Y.1    Tayer, N.2    Rotem, D.3    Schteiber, G.4    Schudiner, S.5
  • 29
    • 76749095057 scopus 로고    scopus 로고
    • Mechanism of substrate recognition and transport by an amino acid antiporter
    • Gao, X. et al. Mechanism of substrate recognition and transport by an amino acid antiporter. Nature 463, 828-832 (2010).
    • (2010) Nature , vol.463 , pp. 828-832
    • Gao, X.1
  • 30
    • 84355166442 scopus 로고    scopus 로고
    • Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket
    • Nakashima, R., Sakurai, K., Yamasaki, S., Nishino, K. & Yamaguchi, A. Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket. Nature 480, 565-569 (2011).
    • (2011) Nature , vol.480 , pp. 565-569
    • Nakashima, R.1    Sakurai, K.2    Yamasaki, S.3    Nishino, K.4    Yamaguchi, A.5
  • 31
    • 84867092080 scopus 로고    scopus 로고
    • Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP
    • Perez, C., Koshy, C., Yildiz, O. & Ziegler, C. Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP. Nature 490, 126-130 (2012).
    • (2012) Nature , vol.490 , pp. 126-130
    • Perez, C.1    Koshy, C.2    Yildiz, O.3    Ziegler, C.4
  • 32
    • 84876297961 scopus 로고    scopus 로고
    • Structural basis for the drug extrusion mechanism by a MATE multidrug transporter
    • Tanaka, Y. et al. Structural basis for the drug extrusion mechanism by a MATE multidrug transporter. Nature 496, 247-251 (2013).
    • (2013) Nature , vol.496 , pp. 247-251
    • Tanaka, Y.1
  • 33
    • 57349141498 scopus 로고    scopus 로고
    • MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II
    • Yamanaka, H., Kobayashi, H., Takahashi, E. & Okamoto, K. MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II. J. Bacteriol. 190, 7693-7698 (2008).
    • (2008) J. Bacteriol. , vol.190 , pp. 7693-7698
    • Yamanaka, H.1    Kobayashi, H.2    Takahashi, E.3    Okamoto, K.4
  • 34
    • 39449086721 scopus 로고    scopus 로고
    • Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances
    • Wiegand, I., Hilpert, K. & Hancock, R.E.W. Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances. Nat. Protoc. 3, 163-175 (2008).
    • (2008) Nat. Protoc. , vol.3 , pp. 163-175
    • Wiegand, I.1    Hilpert, K.2    Hancock, R.E.W.3
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 37
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D Biol. Crystallogr. 57, 1373-1382 (2001).
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 38
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • De La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 39
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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