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Volumn 5, Issue 4, 1998, Pages 294-303

The crystal structure of Dps, a ferritin homolog that binds and protects DNA

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; FERRITIN;

EID: 0031959912     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0498-294     Document Type: Article
Times cited : (460)

References (40)
  • 1
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr, S.B. & Kogoma, T. Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 55 561-585 (1991).
    • (1991) Microbiol. Rev. , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 2
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almirón, M, Link, A.J., Furlong, D. & Kolter, R. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6 2646-2654 (1992).
    • (1992) Genes Dev. , vol.6 , pp. 2646-2654
    • Almirón, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 3
    • 0028181132 scopus 로고
    • 38-dependent expression of a core Escherichia coli starvation gene, pexB
    • 38-dependent expression of a core Escherichia coli starvation gene, pexB. J. Bacteriol. 176 3928-3935 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 3928-3935
    • Lomovskaya, O.L.1    Kidwell, J.P.2    Matin, A.3
  • 4
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • Martinez, A. & Kolter, R. Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J. Bacteriol. 179 5188-5194 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 6
    • 0025153881 scopus 로고
    • More than just 'histone-like' proteins
    • Schmid M.B. More than just 'histone-like' proteins. Cell 63 451-453 (1990).
    • (1990) Cell , vol.63 , pp. 451-453
    • Schmid, M.B.1
  • 7
    • 0029082683 scopus 로고
    • The Dpsa protein of Synecbococcus sp. strain PCC7942 is a DNA-binding hemoprotein
    • Peña, M.O. & Bullerjahn, G.S. The DpsA protein of Synecbococcus sp. strain PCC7942 is a DNA-binding hemoprotein. J. Biol. Chem. 270 22478-22482 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 22478-22482
    • Peña, M.O.1    Bullerjahn, G.S.2
  • 8
    • 0028861959 scopus 로고
    • Bacillus subtilis Mrga is a Dps (PexB) homologue: Evidence for metalloregulation of an oxidative stress gene
    • Chen, L. and Helmann, J.D. Bacillus subtilis MrgA is a Dps (PexB) homologue: evidence for metalloregulation of an oxidative stress gene. Mol. Microbiol. 18 295-300 (1995).
    • (1995) Mol. Microbiol. , vol.18 , pp. 295-300
    • Chen, L.1    Helmann, J.D.2
  • 9
    • 0031032646 scopus 로고    scopus 로고
    • A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Lysteria innocua
    • Bozzi, M. et al. A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Lysteria innocua. J. Biol. Chem. 272 3259-3265 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 3259-3265
    • Bozzi, M.1
  • 10
    • 0030022898 scopus 로고    scopus 로고
    • Fine tangled pili expressed by Haemophilus ducreyi are a novel class of pili
    • Brentiens, R.J., Ketterer, M., Apicella, M.A. & Spinola, S.M. Fine tangled pili expressed by Haemophilus ducreyi are a novel class of pili. J. Bacterol. 178 808-816 (1996).
    • (1996) J. Bacterol. , vol.178 , pp. 808-816
    • Brentiens, R.J.1    Ketterer, M.2    Apicella, M.A.3    Spinola, S.M.4
  • 11
    • 0026694319 scopus 로고
    • Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens
    • Pfiefer, O., Pelletier, I, Altenbuchner, J. & Van Pee, K.-H. Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens. J. Gen. Microbiol. 138 1123-1131 (1992).
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1123-1131
    • Pfiefer, O.1    Pelletier, I.2    Altenbuchner, J.3    Van Pee, K.-H.4
  • 12
    • 0028843199 scopus 로고
    • Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences
    • Evans, D.J., Evans, D.G., Lampert, H.C. & Nahano, H. Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences. Gene 153 123-127 (1995).
    • (1995) Gene , vol.153 , pp. 123-127
    • Evans, D.J.1    Evans, D.G.2    Lampert, H.C.3    Nahano, H.4
  • 13
    • 0022490479 scopus 로고
    • Properties of an ordered ring structure formed by recombinant Treponema pallidum surface antigen 4D
    • Fehniger, T.E., Radolf, J.D. & Lovett, M.A. Properties of an ordered ring structure formed by recombinant Treponema pallidum surface antigen 4D. J. Bacteriol. 165 732-739 (1986).
    • (1986) J. Bacteriol. , vol.165 , pp. 732-739
    • Fehniger, T.E.1    Radolf, J.D.2    Lovett, M.A.3
  • 15
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P.M. & Arosio, P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Act 1275 161-203 (1996).
    • (1996) Biochim. Biophys. Act , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 16
    • 0017803865 scopus 로고
    • Electron density map of apoferritin at 2.8 Å resolution
    • Banyard, S.H., Stammer, D.K. & Harrison, P.M. Electron density map of apoferritin at 2.8 Å resolution. Nature 271 282-284 (1978).
    • (1978) Nature , vol.271 , pp. 282-284
    • Banyard, S.H.1    Stammer, D.K.2    Harrison, P.M.3
  • 17
    • 0028040063 scopus 로고
    • Crystallization and structural analysis of bullfrog red-cell L-subunit ferritins
    • Trikha, J. et al. Crystallization and structural analysis of bullfrog red-cell L-subunit ferritins. Proteins 18 107-118 (1994).
    • (1994) Proteins , vol.18 , pp. 107-118
    • Trikha, J.1
  • 18
    • 0026059720 scopus 로고
    • Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
    • Lawson, D.M. et al. Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature 349 541-544 (1991).
    • (1991) Nature , vol.349 , pp. 541-544
    • Lawson, D.M.1
  • 19
    • 0028467772 scopus 로고
    • Structure of a unique twofold symmetric haem-binding site
    • Frolow, F., Kalb (Gilboa) A.J. & Yariv, J. Structure of a unique twofold symmetric haem-binding site. Nature Struct. Biol. 453-460 (1994).
    • (1994) Nature Struct. Biol. , pp. 453-460
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 20
    • 0029609363 scopus 로고
    • Identification of the feroxidase center of Escherichia coli bacterioferritin
    • Le Brun, N.E. et al. Identification of the feroxidase center of Escherichia coli bacterioferritin. Biochem. J. 312 385-392 (1995).
    • (1995) Biochem. J. , vol.312 , pp. 385-392
    • Le Brun, N.E.1
  • 21
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nichols, A. and Honig, B. A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comput. Chem. 12 435-445 (1991).
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nichols, A.1    Honig, B.2
  • 22
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from interfacial and thermodynamic properties of hydrocarbons
    • Nichols, A., Sharp, K.A. & Honig, B. Protein folding and association: insights from interfacial and thermodynamic properties of hydrocarbons. Proteins 11 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nichols, A.1    Sharp, K.A.2    Honig, B.3
  • 23
    • 0027968068 scopus 로고
    • Improving the sensitivity of progressive multiple alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. & Gibson, T.J. Clustal W: Improving the sensitivity of progressive multiple alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 4673-4680 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3    Clustal, W.4
  • 24
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of an IHF-DNa complex: A protein-induced DNa U-turn
    • Rice, P.A., Yang, S.-W., Mizuuchi, K. Crystal structure of an IHF-DNA complex: a protein-induced DNA U-turn. Cell 87 1295-1306 (1996).
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.-W.2    Mizuuchi, K.3
  • 25
    • 0028900971 scopus 로고
    • Solution structure of the DNA-binding domain of a nucleoid-associated protein, HN-S, from Escherichia coli
    • Shindo, H. et al. Solution structure of the DNA-binding domain of a nucleoid-associated protein, HN-S, from Escherichia coli. FEBS Lett. 360 125-131 (1995).
    • (1995) FEBS Lett. , vol.360 , pp. 125-131
    • Shindo, H.1
  • 26
    • 0021286693 scopus 로고
    • 3 Å resolution structure of a protein with histone-like properties in prokaryotes
    • Tanaka, I., Appelt, K., Dijk, J., White, S.W. & Wilson, K.S. 3 Å resolution structure of a protein with histone-like properties in prokaryotes. Nature 310 376-381 (1984).
    • (1984) Nature , vol.310 , pp. 376-381
    • Tanaka, I.1    Appelt, K.2    Dijk, J.3    White, S.W.4    Wilson, K.S.5
  • 27
    • 0025962021 scopus 로고
    • Three-dimensional structure of the E. coli DNA-binding protein FIS
    • Kostrewa, D. et al. Three-dimensional structure of the E. coli DNA-binding protein FIS. Nature 349 178-180 (1992).
    • (1992) Nature , vol.349 , pp. 178-180
    • Kostrewa, D.1
  • 28
    • 0025939520 scopus 로고
    • The molecular structure of wild-type Fis protein, relationship between mutational changes and recombinatorial enhancer function or DNA binding
    • Yuan, H.S. et al. The molecular structure of wild-type Fis protein, relationship between mutational changes and recombinatorial enhancer function or DNA binding. Proc. Nat. Acad. Sci. USA 88 9558-9562 (1992).
    • (1992) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 9558-9562
    • Yuan, H.S.1
  • 29
    • 0027439390 scopus 로고
    • Atomic structures of of the human immunophilin FKBP-12 complexes with FK-506 and rapamycin
    • Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L. & Clardy, J. Atomic structures of of the human immunophilin FKBP-12 complexes with FK-506 and rapamycin. J. Mol. Biol. 229 105-124 (1993).
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in ocsillation mode
    • Ottwinowski, Z. and Minor, W. Processing of X-ray diffraction data collected in ocsillation mode. Meth. Enz. 276 307-326 (1997).
    • (1997) Meth. Enz. , vol.276 , pp. 307-326
    • Ottwinowski, Z.1    Minor, W.2
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative computational project no. 4
    • Collaborative computational project no. 4 The CCP4 suite: Programs for protein crystallography. Acts Crystallogr. D 50 760-763 (1994).
    • (1994) Acts Crystallogr. D , vol.50 , pp. 760-763
  • 32
    • 0031050735 scopus 로고    scopus 로고
    • Screening for heavy-atom derivatives and obtaining accurate isomorphous differences
    • Rould, M.A. Screening for heavy-atom derivatives and obtaining accurate isomorphous differences. Meth. Enz. 276 461-472 (1997).
    • (1997) Meth. Enz. , vol.276 , pp. 461-472
    • Rould, M.A.1
  • 33
    • 0000195345 scopus 로고
    • Geometric sources of redundancy in intensity data and their use in phase determination
    • Bricogne, G. Geometric sources of redundancy in intensity data and their use in phase determination. Acta Crystallogr. A30 395-495 (1974).
    • (1974) Acta Crystallogr. , vol.A30 , pp. 395-495
    • Bricogne, G.1
  • 35
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones, A.T. Interactive computer graphics: FRODO. Meth. Enz. 115 157-171 (1985).
    • (1985) Meth. Enz. , vol.115 , pp. 157-171
    • Jones, A.T.1
  • 36
    • 10644245781 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, A.T., Zou, Y-J.,Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A42 140-149 (1994).
    • (1994) Acta Crystallogr. , vol.A42 , pp. 140-149
    • Jones, A.T.1    Zou, Y.-J.2    Kjeldgaard, M.3
  • 37
    • 0030501416 scopus 로고    scopus 로고
    • A pseudo-cell based approach to efficient crystallography refinement of viruses
    • Jacobson D.H., Hogle, J.M. & Filman, D.J. A pseudo-cell based approach to efficient crystallography refinement of viruses. Acta Crystallogr. D 52 693-711 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 693-711
    • Jacobson, D.H.1    Hogle, J.M.2    Filman, D.J.3
  • 39
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.