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Volumn 14, Issue 3, 2006, Pages 577-587

Conformational flexibility in the multidrug efflux system protein AcrA

Author keywords

[No Author keywords available]

Indexed keywords

DNA FRAGMENT; METHIONINE; MONOMER; TOLC PROTEIN;

EID: 33644833626     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.11.015     Document Type: Article
Times cited : (230)

References (41)
  • 1
    • 14644397893 scopus 로고    scopus 로고
    • Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli
    • J.R. Aires, and H. Nikaido Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli J. Bacteriol. 187 2005 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
    • H. Akama, M. Kanemaki, M. Yoshimura, T. Tsukihara, T. Kashiwagi, H. Yoneyama, S. Narita, A. Nakagawa, and T. Nakae 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 2004 52816 52819
    • (2004) J. Biol. Chem. , vol.279 , pp. 52816-52819
    • Akama, H.1    Kanemaki, M.2    Yoshimura, M.3    Tsukihara, T.4    Kashiwagi, T.5    Yoneyama, H.6    Narita, S.7    Nakagawa, A.8    Nakae, T.9
  • 3
  • 5
    • 0029064088 scopus 로고
    • High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli
    • N. Budisa, B. Steipe, P. Demange, C. Eckerskorn, J. Kellermann, and R. Huber High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli Eur. J. Biochem. 230 1995 788 796
    • (1995) Eur. J. Biochem. , vol.230 , pp. 788-796
    • Budisa, N.1    Steipe, B.2    Demange, P.3    Eckerskorn, C.4    Kellermann, J.5    Huber, R.6
  • 6
    • 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
  • 7
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • E. de La Fortelle, and G. Bricogne Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods Methods Enzymol. 276 1997 472 494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 9
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of Gram-negative bacteria
    • T. Dinh, I.T. Paulsen, and M.H. Saier Jr. A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of Gram-negative bacteria J. Bacteriol. 176 1994 3825 3831
    • (1994) J. Bacteriol. , vol.176 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier Jr., M.H.3
  • 10
    • 0042838181 scopus 로고    scopus 로고
    • Chimeric analysis of AcrA function reveals the importance of its C-terminal domain in its interaction with the AcrB multidrug efflux pump
    • C.A. Elkins, and H. Nikaido Chimeric analysis of AcrA function reveals the importance of its C-terminal domain in its interaction with the AcrB multidrug efflux pump J. Bacteriol. 185 2003 5349 5356
    • (2003) J. Bacteriol. , vol.185 , pp. 5349-5356
    • Elkins, C.A.1    Nikaido, H.2
  • 13
    • 7644244749 scopus 로고    scopus 로고
    • Genetic evidence for functional interactions between TolC and AcrA proteins of a major antibiotic efflux pump of Escherichia coli
    • H. Gerken, and R. Misra Genetic evidence for functional interactions between TolC and AcrA proteins of a major antibiotic efflux pump of Escherichia coli Mol. Microbiol. 54 2004 620 631
    • (2004) Mol. Microbiol. , vol.54 , pp. 620-631
    • Gerken, H.1    Misra, R.2
  • 15
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • R. Higuchi, B. Krummel, and R.K. Saiki A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions Nucleic Acids Res. 16 1988 7351 7367
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 17
    • 10044231647 scopus 로고    scopus 로고
    • Interaction between the TolC and AcrA proteins of a multidrug efflux system of Escherichia coli
    • F. Husain, M. Humbard, and R. Misra Interaction between the TolC and AcrA proteins of a multidrug efflux system of Escherichia coli J. Bacteriol. 186 2004 8533 8536
    • (2004) J. Bacteriol. , vol.186 , pp. 8533-8536
    • Husain, F.1    Humbard, M.2    Misra, R.3
  • 18
    • 0346749468 scopus 로고    scopus 로고
    • PH-induced conformational changes of AcrA, the membrane fusion protein of Escherichia coli multidrug efflux system
    • H. Ip, K. Stratton, H. Zgurskaya, and J. Liu pH-induced conformational changes of AcrA, the membrane fusion protein of Escherichia coli multidrug efflux system J. Biol. Chem. 278 2003 50474 50482
    • (2003) J. Biol. Chem. , vol.278 , pp. 50474-50482
    • Ip, H.1    Stratton, K.2    Zgurskaya, H.3    Liu, J.4
  • 19
    • 0033515434 scopus 로고    scopus 로고
    • Alignment and structure prediction of divergent protein families: Periplasmic and outer membrane proteins of bacterial efflux pumps
    • J.M. Johnson, and G.M. Church Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps J. Mol. Biol. 287 1999 695 715
    • (1999) J. Mol. Biol. , vol.287 , pp. 695-715
    • Johnson, J.M.1    Church, G.M.2
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta. Crystallogr. A 47 1991 110 119
    • (1991) Acta. Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 21
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • V. Koronakis, A. Sharff, E. Koronakis, B. Luisi, and C. Hughes Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export Nature 405 2000 914 919
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 22
    • 0028926676 scopus 로고
    • Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli
    • D. Ma, D.N. Cook, M. Alberti, N.G. Pon, H. Nikaido, and J.E. Hearst Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli Mol. Microbiol. 16 1995 45 55
    • (1995) Mol. Microbiol. , vol.16 , pp. 45-55
    • Ma, D.1    Cook, D.N.2    Alberti, M.3    Pon, N.G.4    Nikaido, H.5    Hearst, J.E.6
  • 23
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • S. Murakami, R. Nakashima, E. Yamashita, and A. Yamaguchi Crystal structure of bacterial multidrug efflux transporter AcrB Nature 419 2002 587 593
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: Robustness to anisotropy and pseudo-centering and utility for detecting twinning
    • J.E. Padilla, and T.O. Yeates A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning Acta Crystallogr. D Biol. Crystallogr. 59 2003 1124 1130
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2
  • 27
    • 0028365952 scopus 로고
    • Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport
    • M.H. Saier Jr., R. Tam, A. Reizer, and J. Reizer Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport Mol. Microbiol. 11 1994 841 847
    • (1994) Mol. Microbiol. , vol.11 , pp. 841-847
    • Saier Jr., M.H.1    Tam, R.2    Reizer, A.3    Reizer, J.4
  • 28
    • 0027532105 scopus 로고
    • Pitch diversity in α-helical coiled coils
    • J. Seo, and C. Cohen Pitch diversity in α-helical coiled coils Proteins 15 1993 223 234
    • (1993) Proteins , vol.15 , pp. 223-234
    • Seo, J.1    Cohen, C.2
  • 29
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • G. Sheldrick, and T. Schneider SHELXL: high-resolution refinement Methods Enzymol. 277 1997 319 343
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.1    Schneider, T.2
  • 30
    • 23944509010 scopus 로고    scopus 로고
    • Direct interaction of multidrug efflux transporter AcrB and outer membrane channel TolC detected via site-directed disulfide cross-linking
    • N. Tamura, S. Murakami, Y. Oyama, M. Ishiguro, and A. Yamaguchi Direct interaction of multidrug efflux transporter AcrB and outer membrane channel TolC detected via site-directed disulfide cross-linking Biochemistry 44 2005 11115 11121
    • (2005) Biochemistry , vol.44 , pp. 11115-11121
    • Tamura, N.1    Murakami, S.2    Oyama, Y.3    Ishiguro, M.4    Yamaguchi, A.5
  • 31
    • 0028817152 scopus 로고
    • Role of outer membrane barrier in efflux-mediated tetracycline resistance of Escherichia coli
    • D.G. Thanassi, G.S. Suh, and H. Nikaido Role of outer membrane barrier in efflux-mediated tetracycline resistance of Escherichia coli J. Bacteriol. 177 1995 998 1007
    • (1995) J. Bacteriol. , vol.177 , pp. 998-1007
    • Thanassi, D.G.1    Suh, G.S.2    Nikaido, H.3
  • 32
    • 3542998054 scopus 로고    scopus 로고
    • AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex
    • E.B. Tikhonova, and H.I. Zgurskaya AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex J. Biol. Chem. 279 2004 32116 32124
    • (2004) J. Biol. Chem. , vol.279 , pp. 32116-32124
    • Tikhonova, E.B.1    Zgurskaya, H.I.2
  • 33
    • 0036889445 scopus 로고    scopus 로고
    • Chimeric analysis of the multicomponent multidrug efflux transporters from Gram-negative bacteria
    • E.B. Tikhonova, Q. Wang, and H.I. Zgurskaya Chimeric analysis of the multicomponent multidrug efflux transporters from Gram-negative bacteria J. Bacteriol. 184 2002 6499 6507
    • (2002) J. Bacteriol. , vol.184 , pp. 6499-6507
    • Tikhonova, E.B.1    Wang, Q.2    Zgurskaya, H.I.3
  • 34
    • 3242890387 scopus 로고    scopus 로고
    • Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system
    • T. Touze, J. Eswaran, E. Bokma, E. Koronakis, C. Hughes, and V. Koronakis Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system Mol. Microbiol. 53 2004 697 706
    • (2004) Mol. Microbiol. , vol.53 , pp. 697-706
    • Touze, T.1    Eswaran, J.2    Bokma, E.3    Koronakis, E.4    Hughes, C.5    Koronakis, V.6
  • 35
    • 0034680167 scopus 로고    scopus 로고
    • Molecular mechanisms that confer antibacterial drug resistance
    • C. Walsh Molecular mechanisms that confer antibacterial drug resistance Nature 406 2000 775 781
    • (2000) Nature , vol.406 , pp. 775-781
    • Walsh, C.1
  • 36
    • 0035853291 scopus 로고    scopus 로고
    • Socket: A program for identifying and analysing coiled-coil motifs within protein structures
    • J. Walshaw, and D.N. Woolfson Socket: a program for identifying and analysing coiled-coil motifs within protein structures J. Mol. Biol. 307 2001 1427 1450
    • (2001) J. Mol. Biol. , vol.307 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2
  • 37
    • 0034681390 scopus 로고    scopus 로고
    • Function of the membrane fusion protein, MexA, of the MexA, B-OprM efflux pump in Pseudomonas aeruginosa without an anchoring membrane
    • H. Yoneyama, H. Maseda, H. Kamiguchi, and T. Nakae Function of the membrane fusion protein, MexA, of the MexA, B-OprM efflux pump in Pseudomonas aeruginosa without an anchoring membrane J. Biol. Chem. 275 2000 4628 4634
    • (2000) J. Biol. Chem. , vol.275 , pp. 4628-4634
    • Yoneyama, H.1    Maseda, H.2    Kamiguchi, H.3    Nakae, T.4
  • 38
    • 0038670226 scopus 로고    scopus 로고
    • Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump
    • E.W. Yu, G. McDermott, H.I. Zgurskaya, H. Nikaido, and D.E. Koshland Jr. Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump Science 300 2003 976 980
    • (2003) Science , vol.300 , pp. 976-980
    • Yu, E.W.1    McDermott, G.2    Zgurskaya, H.I.3    Nikaido, H.4    Koshland Jr., D.E.5
  • 39
    • 0033534373 scopus 로고    scopus 로고
    • AcrA is a highly asymmetric protein capable of spanning the periplasm
    • H.I. Zgurskaya, and H. Nikaido AcrA is a highly asymmetric protein capable of spanning the periplasm J. Mol. Biol. 285 1999 409 420
    • (1999) J. Mol. Biol. , vol.285 , pp. 409-420
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 40
    • 0033594886 scopus 로고    scopus 로고
    • Bypassing the periplasm: Reconstitution of the AcrAB multidrug efflux pump of Escherichia coli
    • H.I. Zgurskaya, and H. Nikaido Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli Proc. Natl. Acad. Sci. USA 96 1999 7190 7195
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7190-7195
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 41
    • 0033940002 scopus 로고    scopus 로고
    • Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli
    • H.I. Zgurskaya, and H. Nikaido Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli J. Bacteriol. 182 2000 4264 4267
    • (2000) J. Bacteriol. , vol.182 , pp. 4264-4267
    • Zgurskaya, H.I.1    Nikaido, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.