메뉴 건너뛰기




Volumn 23, Issue 18, 2004, Pages 3632-3642

Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis

Author keywords

Antibiotic resistant infection; CylR2; DNA complex; Quorum sensing; Signal transduction

Indexed keywords

CYTOLYSIN; DIMER; DNA BINDING PROTEIN; EXOTOXIN; HELIX LOOP HELIX PROTEIN; PROTEIN CYLR1; PROTEIN CYLR2; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 5044238412     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600367     Document Type: Article
Times cited : (39)

References (55)
  • 1
    • 0024284650 scopus 로고
    • Recognition of a DNA operator by the repressor of phage 434: A view at high resolution
    • Aggarwal AK, Rodgers DW, Drottar M, Ptashne M, Harrison SC (1988) Recognition of a DNA operator by the repressor of phage 434: a view at high resolution. Science 242: 899-907
    • (1988) Science , vol.242 , pp. 899-907
    • Aggarwal, A.K.1    Rodgers, D.W.2    Drottar, M.3    Ptashne, M.4    Harrison, S.C.5
  • 3
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A, Grzesiek S (1993) Methodological advances in protein NMR. Accounts Chem Res 26: 131-138
    • (1993) Accounts Chem Res , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 4
    • 0027146277 scopus 로고
    • Operator sequence context influences amino acid-base-pair interactions in 434 repressor-operator complexes
    • Bell AC, Koudelka GB (1993) Operator sequence context influences amino acid-base-pair interactions in 434 repressor-operator complexes. J Mol Biol 234: 542-553
    • (1993) J Mol Biol , vol.234 , pp. 542-553
    • Bell, A.C.1    Koudelka, G.B.2
  • 5
    • 0029786349 scopus 로고    scopus 로고
    • Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic
    • Booth MC, Bogie CP, Sahl HG, Siezen RJ, Hatter KL, Gilmore MS (1996) Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic. Mol Microbiol 21: 1175-1184
    • (1996) Mol Microbiol , vol.21 , pp. 1175-1184
    • Booth, M.C.1    Bogie, C.P.2    Sahl, H.G.3    Siezen, R.J.4    Hatter, K.L.5    Gilmore, M.S.6
  • 6
    • 0141725789 scopus 로고    scopus 로고
    • The Enterococcus faecalis cytolysin: A novel toxin active against eukaryotic and prokaryotic cells
    • Coburn PS, Gilmore MS (2003) The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells. Cell Microbiol 5: 661-669
    • (2003) Cell Microbiol , vol.5 , pp. 661-669
    • Coburn, P.S.1    Gilmore, M.S.2
  • 7
    • 0032967758 scopus 로고    scopus 로고
    • A novel means of self-protection, unrelated to toxin activation, confers immunity to the bactericidal effects of the Enterococcus faecalis cytolysin
    • Coburn PS, Hancock LE, Booth MC, Gilmore MS (1999) A novel means of self-protection, unrelated to toxin activation, confers immunity to the bactericidal effects of the Enterococcus faecalis cytolysin. Infect Immun 67: 3339-3347
    • (1999) Infect Immun , vol.67 , pp. 3339-3347
    • Coburn, P.S.1    Hancock, L.E.2    Booth, M.C.3    Gilmore, M.S.4
  • 8
    • 0030627548 scopus 로고    scopus 로고
    • Studies of protein-ligand interactions by NMR
    • Craik DJ, Wilce JA (1997) Studies of protein-ligand interactions by NMR. Methods Mol Biol 60: 195-232
    • (1997) Methods Mol Biol , vol.60 , pp. 195-232
    • Craik, D.J.1    Wilce, J.A.2
  • 9
    • 0035094743 scopus 로고    scopus 로고
    • Entering a new phase: Using solvent halide ions in protein structure determination
    • Dauter Z, Dauter M (2001) Entering a new phase: Using solvent halide ions in protein structure determination. Structure 9: R21-R26
    • (2001) Structure , vol.9
    • Dauter, Z.1    Dauter, M.2
  • 10
    • 0034142070 scopus 로고    scopus 로고
    • Novel approach to phasing proteins: Derivatization by short cryo-soaking with halides
    • Dauter Z, Dauter M, Rajashankar KR (2000) Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. Acta Crystallogr Sect D Biol Crystallogr 56: 232-237
    • (2000) Acta Crystallogr Sect D Biol Crystallogr , vol.56 , pp. 232-237
    • Dauter, Z.1    Dauter, M.2    Rajashankar, K.R.3
  • 15
    • 0037471164 scopus 로고    scopus 로고
    • Microbiology: The thin line between gut commensal and pathogen
    • Gilmore MS, Ferretti JJ (2003) Microbiology: the thin line between gut commensal and pathogen. Science 299: 1999-2002
    • (2003) Science , vol.299 , pp. 1999-2002
    • Gilmore, M.S.1    Ferretti, J.J.2
  • 16
    • 0037011936 scopus 로고    scopus 로고
    • Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinduction
    • Haas W, Shepard BD, Gilmore MS (2002) Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinduction. Nature 415: 84-87
    • (2002) Nature , vol.415 , pp. 84-87
    • Haas, W.1    Shepard, B.D.2    Gilmore, M.S.3
  • 18
    • 0038782198 scopus 로고    scopus 로고
    • Molecular analysis of the Enterococcus faecalis serotype 2 polysaccharide determinant
    • Hancock LE, Shepar BD, Gilmore MS (2003) Molecular analysis of the Enterococcus faecalis serotype 2 polysaccharide determinant. J Bacteriol 185: 4393-4401
    • (2003) J Bacteriol , vol.185 , pp. 4393-4401
    • Hancock, L.E.1    Shepar, B.D.2    Gilmore, M.S.3
  • 19
    • 0031760503 scopus 로고    scopus 로고
    • Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
    • Hansen MR, Mueller L, Pardi A (1998) Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions. Nat Struct Biol 5: 1065-1074
    • (1998) Nat Struct Biol , vol.5 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Pardi, A.3
  • 20
    • 0025310356 scopus 로고
    • DNA recognition by proteins with the helix-turn-helix motif
    • Harrison SC, Aggarwal AK (1990) DNA recognition by proteins with the helix-turn-helix motif. Annu Rev Biochem 59: 933-969
    • (1990) Annu Rev Biochem , vol.59 , pp. 933-969
    • Harrison, S.C.1    Aggarwal, A.K.2
  • 21
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch JA (2000) Two-component and phosphorelay signal transduction. Curr Opin Microbiol 3: 165-170
    • (2000) Curr Opin Microbiol , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 22
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233: 123-138
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 23
    • 0031861002 scopus 로고    scopus 로고
    • Multiple-drug resistant Enterococci: The nature of the problem and an agenda for the future
    • Huycke MM, Sahm DF, Gilmore MS (1998) Multiple-drug resistant Enterococci: the nature of the problem and an agenda for the future. Emerg Infect Dis 4: 239-249
    • (1998) Emerg Infect Dis , vol.4 , pp. 239-249
    • Huycke, M.M.1    Sahm, D.F.2    Gilmore, M.S.3
  • 24
    • 0025144608 scopus 로고
    • The growth-inhibitory effect of the Enterococcus faecalis bacteriocin encoded by Pad1 extends to the oral Streptococci
    • Jett BD, Gilmore MS (1990) The growth-inhibitory effect of the Enterococcus faecalis bacteriocin encoded by Pad1 extends to the oral Streptococci. J Dent Res 69: 1640-1645
    • (1990) J Dent Res , vol.69 , pp. 1640-1645
    • Jett, B.D.1    Gilmore, M.S.2
  • 25
    • 34249765651 scopus 로고
    • NMR View - A computer-program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA (1994) NMR View-a computer-program for the visualization and analysis of NMR data. J Biomol NMR 4: 603-614
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 27
    • 0028181137 scopus 로고
    • Monte-Carlo docking of protein-DNA complexes-incorporation of DNA flexibility and experimental-data
    • Knegtel RMA, Boelens R, Kaptein R (1994b) Monte-Carlo docking of protein-DNA complexes-incorporation of DNA flexibility and experimental-data. Protein Eng 7: 761-767
    • (1994) Protein Eng , vol.7 , pp. 761-767
    • Knegtel, R.M.A.1    Boelens, R.2    Kaptein, R.3
  • 28
  • 29
    • 0032514949 scopus 로고    scopus 로고
    • An evolutionary link between sporulation and prophage induction in the structure of a repressor: Anti-repressor complex
    • Lewis RJ, Brannigan JA, Offen WA, Smith I, Wilkinson AJ (1998) An evolutionary link between sporulation and prophage induction in the structure of a repressor: anti-repressor complex. J Mol Biol 283: 907-912
    • (1998) J Mol Biol , vol.283 , pp. 907-912
    • Lewis, R.J.1    Brannigan, J.A.2    Offen, W.A.3    Smith, I.4    Wilkinson, A.J.5
  • 30
    • 0032790081 scopus 로고    scopus 로고
    • XtalView Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee DE (1999) XtalView Xfit-a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 125: 156-165
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 31
    • 0024961628 scopus 로고
    • Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution
    • Mondragon A, Subbiah S, Almo SC, Drottar M, Harrison SC (1989a) Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution. J Mol Biol 205: 189-200
    • (1989) J Mol Biol , vol.205 , pp. 189-200
    • Mondragon, A.1    Subbiah, S.2    Almo, S.C.3    Drottar, M.4    Harrison, S.C.5
  • 32
    • 0024961623 scopus 로고
    • Structure of phage 434 Cro protein at 2.35 Å resolution
    • Mondragon A, Wolberger C, Harrison SC (1989b) Structure of phage 434 Cro protein at 2.35 Å resolution. J Mol Biol 205: 179-188
    • (1989) J Mol Biol , vol.205 , pp. 179-188
    • Mondragon, A.1    Wolberger, C.2    Harrison, S.C.3
  • 33
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilis
    • Mulder FAA, Schipper D, Bott R, Boelens R (1999) Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilis. J Mol Biol 292: 111-123
    • (1999) J Mol Biol , vol.292 , pp. 111-123
    • Mulder, F.A.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4
  • 34
    • 0033623182 scopus 로고    scopus 로고
    • Relationships between enterococcal virulence and antimicrobial resistance
    • Mundy LM, Sahm DF, Gilmore MS (2000) Relationships between enterococcal virulence and antimicrobial resistance. Clin Microbiol Rev 13: 513-522
    • (2000) Clin Microbiol Rev , vol.13 , pp. 513-522
    • Mundy, L.M.1    Sahm, D.F.2    Gilmore, M.S.3
  • 35
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53: 240-255
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 36
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger M, Delaglio F, Bax A (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J Magn Reson 131: 373-378
    • (1998) J Magn Reson , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6: 458-463
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 39
    • 0030596082 scopus 로고    scopus 로고
    • Structural role of a buried salt bridge in the 434 repressor DNA-binding domain
    • Pervushin K, Billeter M, Siegal G, Wuthrich K (1996) Structural role of a buried salt bridge in the 434 repressor DNA-binding domain. J Mol Biol 264: 1002-1012
    • (1996) J Mol Biol , vol.264 , pp. 1002-1012
    • Pervushin, K.1    Billeter, M.2    Siegal, G.3    Wuthrich, K.4
  • 40
    • 0033635869 scopus 로고    scopus 로고
    • Adiabatic TOCSY for C,C and H,H J-transfer
    • Peti W, Griesinger C, Bermel W (2000) Adiabatic TOCSY for C,C and H,H J-transfer. J Biomol NMR 18: 199-205
    • (2000) J Biomol NMR , vol.18 , pp. 199-205
    • Peti, W.1    Griesinger, C.2    Bermel, W.3
  • 41
    • 0031573015 scopus 로고    scopus 로고
    • A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to beta-galactosidase in Gram-positive bacteria
    • Poyart C, Trieu-Cuot P (1997) A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to beta-galactosidase in Gram-positive bacteria. FEMS Microbiol Lett 156: 193-198
    • (1997) FEMS Microbiol Lett , vol.156 , pp. 193-198
    • Poyart, C.1    Trieu-Cuot, P.2
  • 42
    • 0013815214 scopus 로고
    • Stereochemical conformations for polypeptide and protein conformations. II. Allowed conformations for a pair of peptide units
    • Ramakrishnan C, Ramachandran GN (1965) Stereochemical conformations for polypeptide and protein conformations. II. Allowed conformations for a pair of peptide units. Biophys J 5: 909-933
    • (1965) Biophys J , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2
  • 43
    • 4644236093 scopus 로고    scopus 로고
    • Expression, purification, crystallisation and preliminary crystallographic studies of the Enterococcus faecalis cytolysin repressor CylR2
    • Razeto A, Giller K, Haas W, Gilmore MS, Zweckstetter M, Becker S (2004) Expression, purification, crystallisation and preliminary crystallographic studies of the Enterococcus faecalis cytolysin repressor CylR2. Acta Crystallogr D 60: 746-748
    • (2004) Acta Crystallogr D , vol.60 , pp. 746-748
    • Razeto, A.1    Giller, K.2    Haas, W.3    Gilmore, M.S.4    Zweckstetter, M.5    Becker, S.6
  • 44
    • 0037071849 scopus 로고    scopus 로고
    • Modulation of virulence within a pathogenicity island in vancomycin-resistant Enterococcus faecalis
    • Shankar N, Baghdayan AS, Gilmore MS (2002) Modulation of virulence within a pathogenicity island in vancomycin-resistant Enterococcus faecalis. Nature 417: 746-750
    • (2002) Nature , vol.417 , pp. 746-750
    • Shankar, N.1    Baghdayan, A.S.2    Gilmore, M.S.3
  • 45
  • 47
    • 0027337534 scopus 로고
    • The phage 434 OR2/R1-69 complex at 2-5 Å resolution
    • Shimon LJ, Harrison SC (1993) The phage 434 OR2/R1-69 complex at 2-5 Å resolution. J Mol Biol 232: 826-838
    • (1993) J Mol Biol , vol.232 , pp. 826-838
    • Shimon, L.J.1    Harrison, S.C.2
  • 48
    • 0031582086 scopus 로고    scopus 로고
    • Single-chain repressors engineered DNA-binding domains of the phage 434 repressor recognize symmetric or asymmetric DNA operators
    • Simoncsits A, Chen J, Percipalle P, Wang S, Törö I, Pongor S (1997) Single-chain repressors engineered DNA-binding domains of the phage 434 repressor recognize symmetric or asymmetric DNA operators. J Mol Biol 267: 118-131
    • (1997) J Mol Biol , vol.267 , pp. 118-131
    • Simoncsits, A.1    Chen, J.2    Percipalle, P.3    Wang, S.4    Törö, I.5    Pongor, S.6
  • 49
    • 0030698722 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium (vol 278, pg 1111, 1997)
    • Tjandra N, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium (vol 278, pg 1111, 1997). Science 278: 1697-1697
    • (1997) Science , vol.278 , pp. 1697-1697
    • Tjandra, N.1    Bax, A.2
  • 50
    • 0033751564 scopus 로고    scopus 로고
    • Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch
    • Toyoda T, Tin OF, Ito K, Fujiwara T, Kumasaka T, Yamamoto M, Garber MB, Nakamura Y (2000) Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch. RNA-Publ RNA Soc 6: 1432-1444
    • (2000) RNA-Publ RNA Soc , vol.6 , pp. 1432-1444
    • Toyoda, T.1    Tin, O.F.2    Ito, K.3    Fujiwara, T.4    Kumasaka, T.5    Yamamoto, M.6    Garber, M.B.7    Nakamura, Y.8
  • 51
    • 0035282706 scopus 로고    scopus 로고
    • Determination of the binding constants of the centromere protein Cbf1 to all 16 centromere DNAs of Saccharomyces cerevisiae
    • Wieland G, Hemmerich P, Koch M, Stoyan T, Hegemann J, Diekmann S (2001) Determination of the binding constants of the centromere protein Cbf1 to all 16 centromere DNAs of Saccharomyces cerevisiae. Nucleic Acids Res 29: 1054-1060
    • (2001) Nucleic Acids Res , vol.29 , pp. 1054-1060
    • Wieland, G.1    Hemmerich, P.2    Koch, M.3    Stoyan, T.4    Hegemann, J.5    Diekmann, S.6
  • 53
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR
    • Zweckstetter M, Bax A (2000) Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR. J Am Chem Soc 122: 3791-3792
    • (2000) J Am Chem Soc , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 54
    • 0034852135 scopus 로고    scopus 로고
    • Characterization of molecular alignment in aqueous suspensions of Pf1 bacteriophage
    • Zweckstetter M, Bax A (2001) Characterization of molecular alignment in aqueous suspensions of Pf1 bacteriophage. J Biomol NMR 20: 365-377
    • (2001) J Biomol NMR , vol.20 , pp. 365-377
    • Zweckstetter, M.1    Bax, A.2
  • 55
    • 0033375146 scopus 로고    scopus 로고
    • Robust refocusing of C-13 magnetization in multidimensional NMR experiments by adiabatic fast passage pulses
    • Zweckstetter M, Holak TA (1999) Robust refocusing of C-13 magnetization in multidimensional NMR experiments by adiabatic fast passage pulses. J Biomol NMR 15: 331-334
    • (1999) J Biomol NMR , vol.15 , pp. 331-334
    • Zweckstetter, M.1    Holak, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.