메뉴 건너뛰기




Volumn 154, Issue 2, 2003, Pages 69-77

Deciphering the molecular basis of multidrug recognition: Crystal structures of the Staphylococcus aureus multidrug binding transcription regulator QacR

Author keywords

Multidrug recognition; Multisite model; QacR; Repressor; Transcription regulation

Indexed keywords

BACTERIAL PROTEIN; BERBERINE; CRYSTAL VIOLET; DEQUALINIUM; DIMER; ETHIDIUM; GLYCOPROTEIN P; MALACHITE GREEN; MULTIDRUG RESISTANCE PROTEIN; PROTEIN SUBUNIT; QACR PROTEIN; REPRESSOR PROTEIN; RHODAMINE 6G; STRUCTURAL PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 0037342112     PISSN: 09232508     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0923-2508(02)00013-X     Document Type: Short Survey
Times cited : (39)

References (34)
  • 1
    • 0028104421 scopus 로고
    • A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates
    • Ahmed M., Borsch C.M., Taylor S.S., Vazques-Laslop N., Neyfakh A.A. A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates. J. Biol. Chem. 269:1994;28506-28513.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28506-28513
    • Ahmed, M.1    Borsch, C.M.2    Taylor, S.S.3    Vazques-Laslop, N.4    Neyfakh, A.A.5
  • 2
    • 0032792553 scopus 로고    scopus 로고
    • Alteration of the repressor activity of MarR, the negative regulator of the Escherichia coli marRAB locus, by multiple chemicals in vitro
    • Alekshun M.N., Levy S.B. Alteration of the repressor activity of MarR, the negative regulator of the Escherichia coli marRAB locus, by multiple chemicals in vitro. J. Bacteriol. 181:1999;4669-4672.
    • (1999) J. Bacteriol. , vol.181 , pp. 4669-4672
    • Alekshun, M.N.1    Levy, S.B.2
  • 3
    • 0034887133 scopus 로고    scopus 로고
    • The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution
    • Alekshun M.N., Levy S.B., Mealy T.R., Seaton B.A., Head J.S. The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution. Nat. Struct. Biol. 8:2001;710-714.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 710-714
    • Alekshun, M.N.1    Levy, S.B.2    Mealy, T.R.3    Seaton, B.A.4    Head, J.S.5
  • 4
    • 0029548986 scopus 로고
    • Residues important for the function of a multihelical DNA binding domain in the new transcription factor family of Cam and Tet repressors
    • Aramaki H., Yagi N., Suzuki M. Residues important for the function of a multihelical DNA binding domain in the new transcription factor family of Cam and Tet repressors. Protein Eng. 8:1995;1259-1266.
    • (1995) Protein Eng. , vol.8 , pp. 1259-1266
    • Aramaki, H.1    Yagi, N.2    Suzuki, M.3
  • 5
    • 0035079976 scopus 로고    scopus 로고
    • Staphylococcal multidrug efflux protein QacA
    • Brown M.H., Skurray R.A. Staphylococcal multidrug efflux protein QacA. J. Mol. Microbiol. 3:2001;163-170.
    • (2001) J. Mol. Microbiol. , vol.3 , pp. 163-170
    • Brown, M.H.1    Skurray, R.A.2
  • 6
    • 0342424187 scopus 로고    scopus 로고
    • Fast prediction and visualization of protein binding pockets with PASS
    • Brady G.P. Jr., Stouten P.F.W. Fast prediction and visualization of protein binding pockets with PASS. J. Computer-Aided Molecular Design. 14:2000;383-401.
    • (2000) J. Computer-Aided Molecular Design , vol.14 , pp. 383-401
    • Brady G.P., Jr.1    Stouten, P.F.W.2
  • 7
    • 0033558105 scopus 로고    scopus 로고
    • A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug transporter MdfA
    • Egdar R., Bibi E. A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug transporter MdfA. EMBO J. 15:1999;822-832.
    • (1999) EMBO J. , vol.15 , pp. 822-832
    • Egdar, R.1    Bibi, E.2
  • 8
    • 0032541162 scopus 로고    scopus 로고
    • QacR is a repressor protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA
    • Grkovic S., Brown M.H., Roberts N.J., Paulsen I.T., Skurray R.A. QacR is a repressor protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA. J. Biol. Chem. 273:1998;18665-18673.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18665-18673
    • Grkovic, S.1    Brown, M.H.2    Roberts, N.J.3    Paulsen, I.T.4    Skurray, R.A.5
  • 9
    • 0035783036 scopus 로고    scopus 로고
    • Transcriptional regulation of multidrug efflux pumps in bacteria
    • Grkovic S., Brown M.H., Skurray R.A. Transcriptional regulation of multidrug efflux pumps in bacteria. Semin. Cell Devel. Biol. 12:2001;225-237.
    • (2001) Semin. Cell Devel. Biol. , vol.12 , pp. 225-237
    • Grkovic, S.1    Brown, M.H.2    Skurray, R.A.3
  • 10
    • 0035205399 scopus 로고    scopus 로고
    • The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers
    • Grkovic S., Brown M.H., Schumacher M.A., Brennan R.G., Skurray R.A. The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers. J. Bacteriol. 183:2001;7102-7109.
    • (2001) J. Bacteriol. , vol.183 , pp. 7102-7109
    • Grkovic, S.1    Brown, M.H.2    Schumacher, M.A.3    Brennan, R.G.4    Skurray, R.A.5
  • 11
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 12
    • 0028244325 scopus 로고
    • Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance
    • Hinrichs W., Kisker C., Duvel M., Muller A., Tovar K., Hillen W., Saenger W. Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance. Science. 264:1994;418-420.
    • (1994) Science , vol.264 , pp. 418-420
    • Hinrichs, W.1    Kisker, C.2    Duvel, M.3    Muller, A.4    Tovar, K.5    Hillen, W.6    Saenger, W.7
  • 14
    • 0035940473 scopus 로고    scopus 로고
    • Evidence for simultaneous binding of dissimilar substrates by the Escherichia coli multidrug transporter MdfA
    • Lewinson O., Bibi E. Evidence for simultaneous binding of dissimilar substrates by the Escherichia coli multidrug transporter MdfA. Biochemistry. 40:2001;12612-12618.
    • (2001) Biochemistry , vol.40 , pp. 12612-12618
    • Lewinson, O.1    Bibi, E.2
  • 15
    • 0035088330 scopus 로고    scopus 로고
    • In search of native substrates and inhibitors of MDR pumps
    • Lewis K. In search of native substrates and inhibitors of MDR pumps. J. Mol. Microbiol. Biotechnol. 3:2001;247-254.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 247-254
    • Lewis, K.1
  • 17
    • 0033524927 scopus 로고    scopus 로고
    • Bioenergetics of the staphylococcal multidrug export protein, QacA
    • Mitchell B.A., Paulsen I.T., Brown M.H., Skurray R.A. Bioenergetics of the staphylococcal multidrug export protein, QacA. J. Biol. Chem. 274:1999;3541-3548.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3541-3548
    • Mitchell, B.A.1    Paulsen, I.T.2    Brown, M.H.3    Skurray, R.A.4
  • 18
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S., Nakashima R., Yamashita E., Yamaguchi A. 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
  • 19
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • Muth T.R., Schuldiner S. A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE. EMBO J. 17:2000;234-240.
    • (2000) EMBO J. , vol.17 , pp. 234-240
    • Muth, T.R.1    Schuldiner, S.2
  • 20
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B.H. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.H.3
  • 21
    • 0034087676 scopus 로고    scopus 로고
    • Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system
    • Orth P., Schnappinger D., Hillen W., Saenger W., Hinrichs W. Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system. Nat. Struct. Biol. 7:2000;215-219.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 215-219
    • Orth, P.1    Schnappinger, D.2    Hillen, W.3    Saenger, W.4    Hinrichs, W.5
  • 22
    • 0029845047 scopus 로고    scopus 로고
    • Multidrug resistance proteins QacA and QacB from Staphylococcus aureus: Membrane topology and identification of residues involved in substrate specificity
    • Paulsen I.T., Brown M.H., Littlejohn T.G., Mitchell B.A., Skurray R.A. Multidrug resistance proteins QacA and QacB from Staphylococcus aureus: Membrane topology and identification of residues involved in substrate specificity. Proc. Nat. Acad. Sci. USA. 60:1996;575-608.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.60 , pp. 575-608
    • Paulsen, I.T.1    Brown, M.H.2    Littlejohn, T.G.3    Mitchell, B.A.4    Skurray, R.A.5
  • 24
    • 0345035518 scopus 로고    scopus 로고
    • The secondary multidrug transporter LmrP contains multiple drug interacting sites
    • Putnam M., Koole L.A., van Veen H.W., Konings W.N. The secondary multidrug transporter LmrP contains multiple drug interacting sites. Biochemistry. 38:1999;13900-13905.
    • (1999) Biochemistry , vol.38 , pp. 13900-13905
    • Putnam, M.1    Koole, L.A.2    Van Veen, H.W.3    Konings, W.N.4
  • 25
    • 0024556774 scopus 로고
    • Conformational and helicoidal analysis of 30 PS dynamics on the d (CGCGAATTCGCG) double helix: "Curves", dials and windows
    • Ravishankar G., Swaminathan S., Beveridge D.L., Lavery R., Sklenar H. Conformational and helicoidal analysis of 30 PS dynamics on the d (CGCGAATTCGCG) double helix: "Curves", dials and windows. J. Biomol. Struct. Dynam. 6:1989;669-699.
    • (1989) J. Biomol. Struct. Dynam. , vol.6 , pp. 669-699
    • Ravishankar, G.1    Swaminathan, S.2    Beveridge, D.L.3    Lavery, R.4    Sklenar, H.5
  • 29
    • 0036500260 scopus 로고    scopus 로고
    • Structural basis for cooperative DNA binding by two dimers of the multidrug binding protein QacR
    • Schumacher M.A., Miller M.C., Grkovic S., Brown M.H., Skurray R.A., Brennan R.G. Structural basis for cooperative DNA binding by two dimers of the multidrug binding protein QacR. EMBO J. 21:2002;1210-1218.
    • (2002) EMBO J. , vol.21 , pp. 1210-1218
    • Schumacher, M.A.1    Miller, M.C.2    Grkovic, S.3    Brown, M.H.4    Skurray, R.A.5    Brennan, R.G.6
  • 30
    • 0025991731 scopus 로고
    • Azidopine noncompetitively interacts with vinblastine and cyclosporin A binding to P-glycoprotein in multidrug resistant cells
    • Tamai L., Safa A.R. Azidopine noncompetitively interacts with vinblastine and cyclosporin A binding to P-glycoprotein in multidrug resistant cells. J. Biol. Chem. 266:1991;16796-16800.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16796-16800
    • Tamai, L.1    Safa, A.R.2
  • 31
    • 0032518394 scopus 로고    scopus 로고
    • A bacterial antibiotic resistance gene that complements the human multidrug resistance P-glycoprotein gene
    • van Veen H.W., Callaghan R., Soceneantu L., Sardini A., Konings W.N., Higgins C.F. A bacterial antibiotic resistance gene that complements the human multidrug resistance P-glycoprotein gene. Nature. 391:1998;291-295.
    • (1998) Nature , vol.391 , pp. 291-295
    • Van Veen, H.W.1    Callaghan, R.2    Soceneantu, L.3    Sardini, A.4    Konings, W.N.5    Higgins, C.F.6
  • 32
    • 0040436016 scopus 로고    scopus 로고
    • Mechanism of ligand recognition by BmrR, the multidrug-responding transcriptional regulator: Mutational analysis of the ligand-binding site
    • Vazquez-Laslop N., Markham P.N., Neyfakh A.A. Mechanism of ligand recognition by BmrR, the multidrug-responding transcriptional regulator: Mutational analysis of the ligand-binding site. Biochemistry. 38:1999;16925-16931.
    • (1999) Biochemistry , vol.38 , pp. 16925-16931
    • Vazquez-Laslop, N.1    Markham, P.N.2    Neyfakh, A.A.3
  • 34
    • 0035905808 scopus 로고    scopus 로고
    • Crystal structure of the transcription activator BmrR bound to DNA and a drug
    • Zheleznova-Heldwein E.E., Brennan R.G. Crystal structure of the transcription activator BmrR bound to DNA and a drug. Nature. 409:2001;378-382.
    • (2001) Nature , vol.409 , pp. 378-382
    • Zheleznova-Heldwein, E.E.1    Brennan, R.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.