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Volumn 394, Issue 6692, 1998, Pages 502-506

Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex

Author keywords

[No Author keywords available]

Indexed keywords

DIPHTHERIA TOXIN; IRON COMPLEX;

EID: 0032581662     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/28893     Document Type: Article
Times cited : (154)

References (30)
  • 1
    • 0028149973 scopus 로고
    • Iron, DtxR, and the regulation of diphtheria toxin expression
    • Tao, X., Schiering, N., Zeng, H. Y., Ringe, D. & Murphy, J. R. Iron, DtxR, and the regulation of diphtheria toxin expression. Mol. Microbiol. 14, 191-197 (1994).
    • (1994) Mol. Microbiol. , vol.14 , pp. 191-197
    • Tao, X.1    Schiering, N.2    Zeng, H.Y.3    Ringe, D.4    Murphy, J.R.5
  • 2
    • 0028826149 scopus 로고
    • Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae
    • Schiering, N. et al. Structures of the apo-and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae.. Proc. Natl Acad. Sci. USA 92, 9843-9850 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9843-9850
    • Schiering, N.1
  • 3
    • 0029964556 scopus 로고    scopus 로고
    • Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysis
    • Ding, X., Zeng, H., Schiering, N., Ringe, D. & Murphy, J. R. Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysis. Nature Struct. Biol. 3, 382-387 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 382-387
    • Ding, X.1    Zeng, H.2    Schiering, N.3    Ringe, D.4    Murphy, J.R.5
  • 4
    • 0028993911 scopus 로고
    • Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors
    • Qiu, X. et al. Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors. Structure 3, 87-100 (1995).
    • (1995) Structure , vol.3 , pp. 87-100
    • Qiu, X.1
  • 5
    • 0029739483 scopus 로고    scopus 로고
    • High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as a co-repressor
    • Qiu, X., Pohl, E., Holmes, R. K. & Hol, W. G. High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as a co-repressor. Biochemsitry 35, 12292-12302 (1996).
    • (1996) Biochemsitry , vol.35 , pp. 12292-12302
    • Qiu, X.1    Pohl, E.2    Holmes, R.K.3    Hol, W.G.4
  • 6
    • 0026641755 scopus 로고
    • Crystal structure of the met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by β-strands
    • Somers, W. S. & Phillips, S. E. V. Crystal structure of the met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by β-strands. Nature 359, 387-393 (1992).
    • (1992) Nature , vol.359 , pp. 387-393
    • Somers, W.S.1    Phillips, S.E.V.2
  • 7
    • 0026800843 scopus 로고
    • Binding of the metalloregulatory protein DtxR to the diphtheria tox operator requires a divalent heavy metal ion and protects the palindromic sequence from DNase I digestion
    • Tao, X. & Murphy, J. R. Binding of the metalloregulatory protein DtxR to the diphtheria tox operator requires a divalent heavy metal ion and protects the palindromic sequence from DNase I digestion. J. Biol. Chem. 267, 21761-21764 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 21761-21764
    • Tao, X.1    Murphy, J.R.2
  • 8
    • 3543019968 scopus 로고    scopus 로고
    • eds Hacker, J., Rappuoli, R., Alouf, J., Fehernbach, F. & Feer, J. (Fisher Stuttgart, Germany, in the press)
    • Must, L. M., Twiddy, E. M., Sabol, S. Z. & Holmes, R. K. in Bacterial Protein Toxins Vol. 6 (eds Hacker, J., Rappuoli, R., Alouf, J., Fehernbach, F. & Feer, J.) (Fisher Stuttgart, Germany, in the press).
    • Bacterial Protein Toxins , vol.6
    • Must, L.M.1    Twiddy, E.M.2    Sabol, S.Z.3    Holmes, R.K.4
  • 9
    • 0027294003 scopus 로고
    • Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR
    • Tao, X. & Murphy, R. R. Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR. Proc. Natl Acad. Sci. USA 90, 8524-8528 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8524-8528
    • Tao, X.1    Murphy, R.R.2
  • 11
    • 0032584223 scopus 로고    scopus 로고
    • How Cro and λ-repressor distinguish between operators: The structural basis underlying a genetic switch
    • Albright, R. A. & Matthews, B. W. How Cro and λ-repressor distinguish between operators: The structural basis underlying a genetic switch. Proc. Natl Acad. Sci. USA 95, 3431-3436 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3431-3436
    • Albright, R.A.1    Matthews, B.W.2
  • 12
    • 0027210121 scopus 로고
    • Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals
    • Schmitt, M. P. & Holmes, R. K. Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals. Mol. Microbiol. 9, 173-181 (1993).
    • (1993) Mol. Microbiol. , vol.9 , pp. 173-181
    • Schmitt, M.P.1    Holmes, R.K.2
  • 13
    • 0028267429 scopus 로고
    • Characterization of mutations that inactivate the diphtheria toxin repressor gene (dtxR)
    • Wang, Z., Schmitt, M. P. & Holmes, R. K. Characterization of mutations that inactivate the diphtheria toxin repressor gene (dtxR). Infect. Immun. 62, 1600-1608 (1994).
    • (1994) Infect. Immun. , vol.62 , pp. 1600-1608
    • Wang, Z.1    Schmitt, M.P.2    Holmes, R.K.3
  • 14
    • 0029093731 scopus 로고
    • Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers
    • Tao, X., Zeng, H. Y. & Murphy, J. R. Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers. Proc. Natl Acad. Sci. USA 92, 6803-6807 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6803-6807
    • Tao, X.1    Zeng, H.Y.2    Murphy, J.R.3
  • 15
    • 0024294634 scopus 로고
    • Crystal structure of trp repressor/operator complex at atomic resolution
    • Otwinowski, Z. et al. Crystal structure of trp repressor/operator complex at atomic resolution. Nature 335, 321-329 (1988).
    • (1988) Nature , vol.335 , pp. 321-329
    • Otwinowski, Z.1
  • 16
    • 0027372621 scopus 로고
    • Tandem binding in crystals of a trp repressor/operator half-site complex
    • Lawson, C. L. & Carey, J. Tandem binding in crystals of a trp repressor/operator half-site complex. Nature 366, 178-182 (1993).
    • (1993) Nature , vol.366 , pp. 178-182
    • Lawson, C.L.1    Carey, J.2
  • 17
    • 0028286761 scopus 로고
    • The solution structure ot the trp repressor-operator DNA complex
    • Zhang, H. et al. The solution structure ot the trp repressor-operator DNA complex. J. Mol. Biol. 238, 592-614 (1994).
    • (1994) J. Mol. Biol. , vol.238 , pp. 592-614
    • Zhang, H.1
  • 18
    • 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. Meth. Enzymol. 276, 307-326 (1997).
    • (1997) Meth. Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 20
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography Version 3.1
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography Version 3.1. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 21
    • 0023140814 scopus 로고
    • Crystallographic R-factor refinement by molecular dynamics
    • Brünger, A. T., Kuriyan, J. & Karplus, M. Crystallographic R-factor refinement by molecular dynamics. Science 235, 458-460 (1987).
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 22
    • 84945096204 scopus 로고
    • Model bias in macromolecular crystal structures
    • Hodel, A., Kim, S.-H. & Brünger, A. T. Model bias in macromolecular crystal structures. Acta Crystallogr. A 48, 851-858 (1992).
    • (1992) Acta Crystallogr. A , vol.48 , pp. 851-858
    • Hodel, A.1    Kim, S.-H.2    Brünger, A.T.3
  • 23
    • 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
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. & Huber, R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 26
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 27
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae
    • Boyd, J., Oza, M. N. & Murphy, J. R. Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae. Proc. Natl Acad. Sci. USA 87, 5968-5972 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5968-5972
    • Boyd, J.1    Oza, M.N.2    Murphy, J.R.3
  • 28
    • 0024556774 scopus 로고
    • Conformational and helical analysis of 30ps of molecular dynamics on the d(CGCGAATTCGCG) double helix: 'Curves', dials and windows
    • Ravishankar, G., Swaminathan, S., Beveridge, D. L., Lavery, R. & Sklenar, H. Conformational and helical analysis of 30ps of molecular dynamics on the d(CGCGAATTCGCG) double helix: 'Curves', dials and windows. J. Biomol. Struct. Dynam. 6, 669-699 (1989).
    • (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
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program package to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: A program package to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R. J. Improved fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149 (1986).
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1


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