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Volumn 193, Issue 10, 2011, Pages 2381-2387

Switch or funnel: How RND-type transport systems control periplasmic metal homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORTER; HEAVY METAL; MEMBRANE FUSION PROTEIN; OUTER MEMBRANE PROTEIN; PERIPLASMIC PROTEIN; PROTON;

EID: 79956087446     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01323-10     Document Type: Short Survey
Times cited : (119)

References (59)
  • 1
    • 14644397893 scopus 로고    scopus 로고
    • Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli
    • Aires, J. R., and H. Nikaido. 2005. Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli. J. Bacteriol. 187:1923-1929.
    • (2005) J. Bacteriol. , vol.187 , pp. 1923-1929
    • Aires, J.R.1    Nikaido, H.2
  • 2
    • 11144222920 scopus 로고    scopus 로고
    • Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end
    • Akama, H., et al. 2004. Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J. Biol. Chem. 279:52816-52819.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52816-52819
    • Akama, H.1
  • 3
    • 2942731519 scopus 로고    scopus 로고
    • Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa
    • Akama, H., et al. 2004. Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa. J. Biol. Chem. 279:25939-25942.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25939-25942
    • Akama, H.1
  • 4
    • 0037143615 scopus 로고    scopus 로고
    • Transition to the open state of the TolC periplasmic tunnel entrance
    • Andersen, C., et al. 2002. Transition to the open state of the TolC periplasmic tunnel entrance. Proc. Natl. Acad. Sci. U. S. A. 99:11103-11108.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11103-11108
    • Andersen, C.1
  • 5
    • 37249081439 scopus 로고    scopus 로고
    • Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system
    • Bagai, I., W. Liu, C. Rensing, N. J. Blackburn, and M. M. McEvoy. 2007. Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system. J. Biol. Chem. 282:35695-35702.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35695-35702
    • Bagai, I.1    Liu, W.2    Rensing, C.3    Blackburn, N.J.4    McEvoy, M.M.5
  • 6
    • 55249109759 scopus 로고    scopus 로고
    • Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone
    • Bagai, I., C. Rensing, N. J. Blackburn, and M. M. McEvoy. 2008. Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry 47:11408-11414.
    • (2008) Biochemistry , vol.47 , pp. 11408-11414
    • Bagai, I.1    Rensing, C.2    Blackburn, N.J.3    McEvoy, M.M.4
  • 7
    • 77951297882 scopus 로고    scopus 로고
    • Evidence that the C-terminus of OprM is involved in the assembly of the VceAB-OprM efflux pump
    • Bai, J., L. Mosley, and J. A. Fralick. 2010. Evidence that the C-terminus of OprM is involved in the assembly of the VceAB-OprM efflux pump. FEBS Lett. 584:1493-1497.
    • (2010) FEBS Lett , vol.584 , pp. 1493-1497
    • Bai, J.1    Mosley, L.2    Fralick, J.A.3
  • 8
    • 41549158741 scopus 로고    scopus 로고
    • Assembly and channel opening in a bacterial drug efflux machine
    • Bavro, V. N., et al. 2008. Assembly and channel opening in a bacterial drug efflux machine. Mol. Cell 30:114-121.
    • (2008) Mol. Cell , vol.30 , pp. 114-121
    • Bavro, V.N.1
  • 9
    • 77953500303 scopus 로고    scopus 로고
    • Differing ability to transport nonmetal substrates by two RND-type metal exporters
    • Conroy, O., E. H. Kim, M. M. McEvoy, and C. Rensing. 2010. Differing ability to transport nonmetal substrates by two RND-type metal exporters. FEMS Microbiol. Lett. 308:115-122.
    • (2010) FEMS Microbiol. Lett. , vol.308 , pp. 115-122
    • Conroy, O.1    Kim, E.H.2    McEvoy, M.M.3    Rensing, C.4
  • 10
    • 34248572735 scopus 로고    scopus 로고
    • Crystal structure of the multidrug efflux transporter AcrB at 3.1A resolution reveals the N-terminal region with conserved amino acids
    • Das, D., et al. 2007. Crystal structure of the multidrug efflux transporter AcrB at 3.1A resolution reveals the N-terminal region with conserved amino acids. J. Struct. Biol. 158:494-502.
    • (2007) J. Struct. Biol. , vol.158 , pp. 494-502
    • Das, D.1
  • 11
    • 77954656149 scopus 로고    scopus 로고
    • Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems
    • De Angelis, F., et al. 2010. Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems. Proc. Natl. Acad. Sci. U. S. A. 107:11038-11043.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 11038-11043
    • De Angelis, F.1
  • 12
    • 15344343162 scopus 로고    scopus 로고
    • Role of the extracytoplasmic function protein family sigma factor RpoE in metal resistance of Escherichia coli
    • Egler, M., C. Grosse, G. Grass, and D. H. Nies. 2005. Role of the extracytoplasmic function protein family sigma factor RpoE in metal resistance of Escherichia coli. J. Bacteriol. 187:2297-2307.
    • (2005) J. Bacteriol. , vol.187 , pp. 2297-2307
    • Egler, M.1    Grosse, C.2    Grass, G.3    Nies, D.H.4
  • 13
    • 0037701544 scopus 로고    scopus 로고
    • Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli
    • Franke, S., G. Grass, C. Rensing, and D. H. Nies. 2003. Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli. J. Bacteriol. 185:3804-3812.
    • (2003) J. Bacteriol. , vol.185 , pp. 3804-3812
    • Franke, S.1    Grass, G.2    Rensing, C.3    Nies, D.H.4
  • 14
    • 0033543578 scopus 로고    scopus 로고
    • Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulationcell division protein family
    • Goldberg, M., T. Pribyl, S. Juhnke, and D. H. Nies.1999. Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulationcell division protein family. J. Biol. Chem. 274:26065-26070.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26065-26070
    • Goldberg, M.1    Pribyl, T.2    Juhnke, S.3    Nies, D.H.4
  • 15
    • 0034817086 scopus 로고    scopus 로고
    • CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli
    • Grass, G., and C. Rensing. 2001. CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli. Biochem. Biophys. Res. Commun. 286: 902-908.
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 902-908
    • Grass, G.1    Rensing, C.2
  • 16
    • 77951991586 scopus 로고    scopus 로고
    • Chaperone-mediated copper handling in the periplasm
    • Kim, E.-H., C. Rensing, and M. M. McEvoy. 2010. Chaperone-mediated copper handling in the periplasm. Nat. Prod. Rep. 27:711-719.
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 711-719
    • Kim, E.-H.1    Rensing, C.2    McEvoy, M.M.3
  • 17
    • 77956524004 scopus 로고    scopus 로고
    • Functional relationships between the AcrA hairpin tip region and the TolC aperture tip region for the formation of the bacterial tripartite efflux pump AcrAB-TolC
    • Kim, H. M., et al. 2010. Functional relationships between the AcrA hairpin tip region and the TolC aperture tip region for the formation of the bacterial tripartite efflux pump AcrAB-TolC. J. Bacteriol.192:4498-4503.
    • (2010) J. Bacteriol , vol.192 , pp. 4498-4503
    • Kim, H.M.1
  • 18
    • 77749279768 scopus 로고    scopus 로고
    • Multidrug efflux pump MdtBC of Escherichia coli is active only as a B2C heterotrimer
    • Kim, H. S., D. Nagore, and H. Nikaido. 2010. Multidrug efflux pump MdtBC of Escherichia coli is active only as a B2C heterotrimer. J. Bacteriol.192: 1377-1386.
    • (2010) J. Bacteriol , vol.192 , pp. 1377-1386
    • Kim, H.S.1    Nagore, D.2    Nikaido, H.3
  • 19
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis, V., A. Sharff, E. Koronakis, B. Luisi, and C. Hughes. 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
  • 20
    • 79251563176 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump
    • Kulathila, R., M. Indic, and B. van den Berg. 2011. Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump. PLoS One 6:e15610.
    • (2011) PLoS One , vol.6
    • Kulathila, R.1    Indic, M.2    van den Berg, B.3
  • 21
    • 0038713357 scopus 로고    scopus 로고
    • First step towards a quantitative model describing Czc-mediated heavy metal resistance in Ralstonia metallidurans
    • Legatzki, A., et al. 2003. First step towards a quantitative model describing Czc-mediated heavy metal resistance in Ralstonia metallidurans. Biodegradation 14:153-168.
    • (2003) Biodegradation , vol.14 , pp. 153-168
    • Legatzki, A.1
  • 22
    • 0038444418 scopus 로고    scopus 로고
    • Interplay of the Czc system and two P-type ATPases in conferring metal resistance to Ralstonia metallidurans
    • Legatzki, A., G. Grass, A. Anton, C. Rensing, and D. H. Nies. 2003. Interplay of the Czc system and two P-type ATPases in conferring metal resistance to Ralstonia metallidurans. J. Bacteriol. 185:4354-4361.
    • (2003) J. Bacteriol. , vol.185 , pp. 4354-4361
    • Legatzki, A.1    Grass, G.2    Anton, A.3    Rensing, C.4    Nies, D.H.5
  • 23
    • 23244451021 scopus 로고    scopus 로고
    • A novel copper-binding fold for the periplasmic copper resistance protein CusF
    • Loftin, I. R., et al. 2005. A novel copper-binding fold for the periplasmic copper resistance protein CusF. Biochemistry 44:10533-10540.
    • (2005) Biochemistry , vol.44 , pp. 10533-10540
    • Loftin, I.R.1
  • 24
    • 77957141422 scopus 로고    scopus 로고
    • Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport
    • Long, F., et al. 2010. Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature 467:484-488.
    • (2010) Nature , vol.467 , pp. 484-488
    • Long, F.1
  • 25
    • 70350637580 scopus 로고    scopus 로고
    • Coordination chemistry of bacterial metal transport and sensing
    • Ma, Z., F. E. Jacobsen, and D. P. Giedroc. 2009. Coordination chemistry of bacterial metal transport and sensing. Chem. Rev. 109:4644-4681.
    • (2009) Chem. Rev. , vol.109 , pp. 4644-4681
    • Ma, Z.1    Jacobsen, F.E.2    Giedroc, D.P.3
  • 26
    • 64649089196 scopus 로고    scopus 로고
    • Assembly and transport mechanism of tripartite drug efflux systems
    • Misra, R., and V. N. Bavro. 2009. Assembly and transport mechanism of tripartite drug efflux systems. Biochim. Biophys. Acta 1794:817-825.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 817-825
    • Misra, R.1    Bavro, V.N.2
  • 27
    • 9244224655 scopus 로고    scopus 로고
    • The chromosomally encoded cation diffusion facilitator proteins DmeF and FieF from Wautersia metallidurans CH34 are transporters of broad metal specificity
    • Munkelt, D., G. Grass, and D. H. Nies. 2004. The chromosomally encoded cation diffusion facilitator proteins DmeF and FieF from Wautersia metallidurans CH34 are transporters of broad metal specificity. J. Bacteriol. 186: 8036-8043.
    • (2004) J. Bacteriol. , vol.186 , pp. 8036-8043
    • Munkelt, D.1    Grass, G.2    Nies, D.H.3
  • 28
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • Murakami, S., R. Nakashima, E. Yamashita, T. Matsumoto, and A. Yamaguchi. 2006. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443:173-179.
    • (2006) Nature , vol.443 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 29
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami, S., R. Nakashima, E. Yamashita, and A. Yamaguchi. 2002. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419:587-593.
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 31
    • 34648819082 scopus 로고    scopus 로고
    • Biochemistry. How cells control zinc homeostasis
    • Nies, D. H. 2007. Biochemistry. How cells control zinc homeostasis. Science 317:1695-1696.
    • (2007) Science , vol.317 , pp. 1695-1696
    • Nies, D.H.1
  • 32
    • 0029016714 scopus 로고
    • The cobalt, zinc, and cadmium efflux system CzcABC from Alcaligenes eutrophus functions as a cation-proton antiporter in Escherichia coli
    • Nies, D. H.1995. The cobalt, zinc, and cadmium efflux system CzcABC from Alcaligenes eutrophus functions as a cation-proton antiporter in Escherichia coli. J. Bacteriol. 177:2707-2712.
    • (1995) J. Bacteriol. , vol.177 , pp. 2707-2712
    • Nies, D.H.1
  • 33
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies, D. H. 2003. Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol. Rev. 27:313-339.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 313-339
    • Nies, D.H.1
  • 34
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten, C. E., and T. V. O'Halloran. 2001. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292:2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 35
    • 0035903128 scopus 로고    scopus 로고
    • The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli
    • Outten, F. W., D. L. Huffman, J. A. Hale, and T. V. O'Halloran. 2001. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J. Biol. Chem. 276:30670-30677.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30670-30677
    • Outten, F.W.1    Huffman, D.L.2    Hale, J.A.3    O'Halloran, T.V.4
  • 36
    • 0031278034 scopus 로고    scopus 로고
    • A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from gram-negative bacteria
    • Paulsen, I. T., J. H. Park, P. S. Choi, and M. H. Saier.1997. A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from gram-negative bacteria. FEMS Microbiol. Lett. 156:1-8.
    • (1997) FEMS Microbiol. Lett. , vol.156 , pp. 1-8
    • Paulsen, I.T.1    Park, J.H.2    Choi, P.S.3    Saier, M.H.4
  • 37
    • 0017648660 scopus 로고
    • New types of mutation affecting formation of alkaline phosphatase by Bacillus subtilis in sporulation conditions
    • Piggot, P. J., and S. Y. Taylor.1977. New types of mutation affecting formation of alkaline phosphatase by Bacillus subtilis in sporulation conditions. J. Gen. Microbiol. 102:69-80.
    • (1977) J. Gen. Microbiol. , vol.102 , pp. 69-80
    • Piggot, P.J.1    Taylor, S.Y.2
  • 38
    • 64649100965 scopus 로고    scopus 로고
    • Drug transport mechanism of the AcrB efflux pump
    • Pos, K. M. 2009. Drug transport mechanism of the AcrB efflux pump. Biochim. Biophys. Acta 1794:782-793.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 782-793
    • Pos, K.M.1
  • 40
    • 0037565099 scopus 로고    scopus 로고
    • Escherichia coli mechanisms of copper homeostasis in a changing environment
    • Rensing, C., and G. Grass. 2003. Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol. Rev. 27:197-213.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 197-213
    • Rensing, C.1    Grass, G.2
  • 41
    • 0030817267 scopus 로고    scopus 로고
    • New functions for the three subunits of the CzcCBA cation-proton antiporter
    • Rensing, C., T. Pribyl, and D. H. Nies.1997. New functions for the three subunits of the CzcCBA cation-proton antiporter. J. Bacteriol. 179:6871-6879.
    • (1997) J. Bacteriol. , vol.179 , pp. 6871-6879
    • Rensing, C.1    Pribyl, T.2    Nies, D.H.3
  • 42
    • 0037022682 scopus 로고    scopus 로고
    • Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli
    • Roberts, S. A., et al. 2002. Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 99:2766-2771.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2766-2771
    • Roberts, S.A.1
  • 43
    • 77956907517 scopus 로고    scopus 로고
    • Methionine motifs of copper transport proteins provide general and flexible thioether-only binding sites for Cu(I) and Ag(I)
    • Rubino, J. T., P. Riggs-Gelasco, and K. J. Franz. 2010. Methionine motifs of copper transport proteins provide general and flexible thioether-only binding sites for Cu(I) and Ag(I). J. Biol. Inorg Chem. 15:1033-1049.
    • (2010) J. Biol. Inorg Chem. , vol.15 , pp. 1033-1049
    • Rubino, J.T.1    Riggs-Gelasco, P.2    Franz, K.J.3
  • 44
    • 0028365952 scopus 로고
    • Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport
    • Saier, M. H., R. Tam, A. Reizer, and J. Reizer.1994. Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Mol. Microbiol. 11:841-847.
    • (1994) Mol. Microbiol. , vol.11 , pp. 841-847
    • Saier, M.H.1    Tam, R.2    Reizer, A.3    Reizer, J.4
  • 45
    • 70350146566 scopus 로고    scopus 로고
    • CzcP is a novel efflux system contributing to transition metal resistance in Cupriavidus metallidurans CH34
    • Scherer, J., and D. H. Nies. 2009. CzcP is a novel efflux system contributing to transition metal resistance in Cupriavidus metallidurans CH34. Mol. Microbiol. 73:601-621.
    • (2009) Mol. Microbiol. , vol.73 , pp. 601-621
    • Scherer, J.1    Nies, D.H.2
  • 47
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • Seeger, M. A., et al. 2006. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313:1295-1298.
    • (2006) Science , vol.313 , pp. 1295-1298
    • Seeger, M.A.1
  • 48
    • 65449155090 scopus 로고    scopus 로고
    • Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa
    • Sennhauser, G., M. A. Bukowska, C. Briand, and M. G. Grutter. 2009. Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa. J. Mol. Biol. 389:134-145.
    • (2009) J. Mol. Biol. , vol.389 , pp. 134-145
    • Sennhauser, G.1    Bukowska, M.A.2    Briand, C.3    Grutter, M.G.4
  • 49
    • 7744237723 scopus 로고    scopus 로고
    • Cuprous oxidase activity of CueO from Escherichia coli
    • Singh, S. K., G. Grass, C. Rensing, and W. R. Montfort. 2004. Cuprous oxidase activity of CueO from Escherichia coli. J. Bacteriol. 186:7815-7817.
    • (2004) J. Bacteriol. , vol.186 , pp. 7815-7817
    • Singh, S.K.1    Grass, G.2    Rensing, C.3    Montfort, W.R.4
  • 50
    • 33748638824 scopus 로고    scopus 로고
    • Importance of the adaptor (membrane fusion) protein hairpin domain for the functionality of multidrug efflux pumps
    • Stegmeier, J. F., G. Polleichtner, N. Brandes, C. Hotz, and C. Andersen. 2006. Importance of the adaptor (membrane fusion) protein hairpin domain for the functionality of multidrug efflux pumps. Biochemistry 45:10303-10312.
    • (2006) Biochemistry , vol.45 , pp. 10303-10312
    • Stegmeier, J.F.1    Polleichtner, G.2    Brandes, N.3    Hotz, C.4    Andersen, C.5
  • 51
    • 78650791250 scopus 로고    scopus 로고
    • The Cus efflux system removes toxic ions via a methionine shuttle
    • Su, C. C., F. Long, and E. W. Yu. 2011. The Cus efflux system removes toxic ions via a methionine shuttle. Protein Sci. 20:6-18.
    • (2011) Protein Sci. , vol.20 , pp. 6-18
    • Su, C.C.1    Long, F.2    Yu, E.W.3
  • 52
    • 70349558132 scopus 로고    scopus 로고
    • Crystal structure of the membrane fusion protein CusB from Escherichia coli
    • Su, C. C., et al. 2009. Crystal structure of the membrane fusion protein CusB from Escherichia coli. J. Mol. Biol. 393:342-355.
    • (2009) J. Mol. Biol. , vol.393 , pp. 342-355
    • Su, C.C.1
  • 54
    • 23644449395 scopus 로고    scopus 로고
    • Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism
    • Teplyakov, A., G. Obmolova, J. Toedt, M. Y. Galperin, and G. L. Gilliland. 2005. Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism. J. Bacteriol. 187:5520-5527.
    • (2005) J. Bacteriol. , vol.187 , pp. 5520-5527
    • Teplyakov, A.1    Obmolova, G.2    Toedt, J.3    Galperin, M.Y.4    Gilliland, G.L.5
  • 55
    • 0033170990 scopus 로고    scopus 로고
    • The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins
    • Tseng, T. T., et al.1999. The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J. Mol. Microbiol. Biotechnol. 1:107-125.
    • (1999) J. Mol. Microbiol. Biotechnol. , vol.1 , pp. 107-125
    • Tseng, T.T.1
  • 56
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal? Nat
    • Waldron, K. J., and N. J. Robinson. 2009. How do bacterial cells ensure that metalloproteins get the correct metal? Nat. Rev. Microbiol. 7:25-35.
    • (2009) Rev. Microbiol. , vol.7 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2
  • 57
    • 77949360141 scopus 로고    scopus 로고
    • AcrA suppressor alterations reverse the drug hypersensitivity phenotype of a TolC mutant by inducing TolC aperture opening
    • Weeks, J. W., T. Celaya-Kolb, S. Pecora, and R. Misra. 2010. AcrA suppressor alterations reverse the drug hypersensitivity phenotype of a TolC mutant by inducing TolC aperture opening. Mol. Microbiol. 75:1468-1483.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1468-1483
    • Weeks, J.W.1    Celaya-Kolb, T.2    Pecora, S.3    Misra, R.4
  • 58
    • 77956700488 scopus 로고    scopus 로고
    • Promiscuous partnering and independent activity of MexB, the multidrug transporter protein from Pseudomonas aeruginosa
    • Welch, A., C. U. Awah, S. Jing, H. W. van Veen, and H. Venter. 2010. Promiscuous partnering and independent activity of MexB, the multidrug transporter protein from Pseudomonas aeruginosa. Biochem. J. 430:355-364.
    • (2010) Biochem. J. , vol.430 , pp. 355-364
    • Welch, A.1    Awah, C.U.2    Jing, S.3    van Veen, H.W.4    Venter, H.5
  • 59
    • 25144504245 scopus 로고    scopus 로고
    • A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study
    • Yu, E. W., J. R. Aires, G. McDermott, and H. Nikaido. 2005. A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study. J. Bacteriol. 187:6804-6815.
    • (2005) J. Bacteriol. , vol.187 , pp. 6804-6815
    • Yu, E.W.1    Aires, J.R.2    McDermott, G.3    Nikaido, H.4


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