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Volumn 4, Issue 11, 1997, Pages 919-924

Structure of Haemophilus influenzae Fe+3-binding protein reveals convergent evolution within a superfamily

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; FERRIC ION; IRON BINDING PROTEIN; TRANSFERRIN;

EID: 0030691197     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1197-919     Document Type: Article
Times cited : (167)

References (31)
  • 1
    • 0021190269 scopus 로고
    • The relationship of plasmid-mediated iron transport and bacterial virulence
    • Crosa, J.H. The relationship of plasmid-mediated iron transport and bacterial virulence. Annu. Rev. Microbiol. 38, 69-89 (1984).
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 69-89
    • Crosa, J.H.1
  • 2
    • 0021356806 scopus 로고
    • Iron withholding: A defense against infection and neoplasia
    • Weinberg, E.D. Iron withholding: A defense against infection and neoplasia. Physiol. Rev. 64(1), 65-102 (1984).
    • (1984) Physiol. Rev. , vol.64 , Issue.1 , pp. 65-102
    • Weinberg, E.D.1
  • 4
    • 0028846011 scopus 로고
    • Biochemical characterization of a Haemophilus influenzae periplasmic iron transport operon
    • Adhikari, P. et al. Biochemical characterization of a Haemophilus influenzae periplasmic iron transport operon. J. Biol. Chem. 270, 25142-25149 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25142-25149
    • Adhikari, P.1
  • 5
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R. & Saier, M.H.J. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57, 320-346 (1993).
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier, M.H.J.2
  • 6
    • 0001150127 scopus 로고
    • Structure of human lactoferrin at 3.2 Å resolution
    • Anderson, B.F. et al. Structure of human lactoferrin at 3.2 Å resolution. Proc. Natl. Acad. Sci. USA 84, 1769-1773 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1769-1773
    • Anderson, B.F.1
  • 7
    • 0023793522 scopus 로고
    • Molecular structure of serum transferrin at 33 Å resolution
    • Bailey, S. et al. Molecular structure of serum transferrin at 33 Å resolution. Biochemistry 27, 5804-5812 (1988).
    • (1988) Biochemistry , vol.27 , pp. 5804-5812
    • Bailey, S.1
  • 8
    • 0021804775 scopus 로고
    • Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds
    • Pflugrath, J. & Quiocho, F. Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds. Nature 314, 257-260 (1985).
    • (1985) Nature , vol.314 , pp. 257-260
    • Pflugrath, J.1    Quiocho, F.2
  • 9
    • 0024464164 scopus 로고
    • Bacterial periplasmic binding protein tertiary structures
    • Adams, M.D. & Oxender, D.L. Bacterial periplasmic binding protein tertiary structures. J. Biol. Chem. 264(27), 15739-15742 (1989).
    • (1989) J. Biol. Chem. , vol.264 , Issue.27 , pp. 15739-15742
    • Adams, M.D.1    Oxender, D.L.2
  • 10
    • 0025716317 scopus 로고
    • Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria
    • Quiocho, F.A. Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria. Phil. Trans. Royal Soc. London B326(1236), 341-351 (1990).
    • (1990) Phil. Trans. Royal Soc. London , vol.B326 , Issue.1236 , pp. 341-351
    • Quiocho, F.A.1
  • 11
    • 0028073139 scopus 로고
    • Coordination of iron by the ferric iron-binding protein of pathogenic Neisseria is homologous to the transferrins
    • Nowalk, A.J., Tencza, S.B. & Mietzner, T.A. Coordination of iron by the ferric iron-binding protein of pathogenic Neisseria is homologous to the transferrins. Biochemistry. 33(43), 12769-12775 (1994).
    • (1994) Biochemistry , vol.33 , Issue.43 , pp. 12769-12775
    • Nowalk, A.J.1    Tencza, S.B.2    Mietzner, T.A.3
  • 12
    • 0024042264 scopus 로고
    • A potential role for the major iron regulated protein expressed by pathogenic Neisseria spp
    • Morse, S., Chen, C., Le Faou, A. & Mietzner, T. A potential role for the major iron regulated protein expressed by pathogenic Neisseria spp. Rev. Infect. Dis. 10(supp), 306-310 (1988).
    • (1988) Rev. Infect. Dis. , vol.10 , Issue.SUPPL. , pp. 306-310
    • Morse, S.1    Chen, C.2    Le Faou, A.3    Mietzner, T.4
  • 13
    • 0025000575 scopus 로고
    • High specificity of a phosphate transport protein determined by hydrogen bonds
    • Luecke, H. & Quiocho, F.A. High specificity of a phosphate transport protein determined by hydrogen bonds. Nature 347, 402-406 (1990).
    • (1990) Nature , vol.347 , pp. 402-406
    • Luecke, H.1    Quiocho, F.A.2
  • 14
    • 0028027510 scopus 로고
    • Fine tuning the specificity of the periplasmic phosphate transport receptor: Site-directed mutagenesis, ligand binding, and crystallographic studies
    • Wang, Z., Choudhary, A., Ledvina, P.S. & Quiocho, F.A. Fine tuning the specificity of the periplasmic phosphate transport receptor: site-directed mutagenesis, ligand binding, and crystallographic studies. J. Biol. Chem. 269, 25091-25094 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 25091-25094
    • Wang, Z.1    Choudhary, A.2    Ledvina, P.S.3    Quiocho, F.A.4
  • 15
    • 0001447664 scopus 로고
    • Transferrins: Insights into structure and function from studies on lactoferrin
    • Baker, E.N., Rumball, S.V. & Anderson, B.F. Transferrins: insights into structure and function from studies on lactoferrin. TIBS 12, 350-353 (1987).
    • (1987) TIBS , vol.12 , pp. 350-353
    • Baker, E.N.1    Rumball, S.V.2    Anderson, B.F.3
  • 17
    • 0027360843 scopus 로고
    • Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: Implications for transferrin iron release
    • Dewan, J.C., Mikami, B., Hirose, M. & Sacchettini, J.C. Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release. Biochemistry. 32, 11963-11968 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11963-11968
    • Dewan, J.C.1    Mikami, B.2    Hirose, M.3    Sacchettini, J.C.4
  • 18
    • 0029051878 scopus 로고
    • Antibiotic resistance in bacteria
    • Berkowitz, F. Antibiotic resistance in bacteria. Southern Medical Journal 88, 797-804 (1995).
    • (1995) Southern Medical Journal , vol.88 , pp. 797-804
    • Berkowitz, F.1
  • 20
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S., Hunt, H., Horton, R., Pullen, J. & Pease, L. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 (1989).
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.1    Hunt, H.2    Horton, R.3    Pullen, J.4    Pease, L.5
  • 21
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/Xview
    • McRee, D.E. A visual protein crystallographic software system for X11/Xview. J. Mol. Graphics 10, 44-46 (1992).
    • (1992) J. Mol. Graphics , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 22
    • 0002701928 scopus 로고
    • Phases: A program package for the processing and analysis of diffraction data from macromolecules
    • Furey, W. & Swaminathan, S. Phases: A program package for the processing and analysis of diffraction data from macromolecules. In: ACA Meeting Abstracts (1990).
    • (1990) ACA Meeting Abstracts
    • Furey, W.1    Swaminathan, S.2
  • 23
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modification calculations
    • Cowtan, K.D. & Main, P. Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr. D52, 43-48 (1996).
    • (1996) Acta Crystallogr. , vol.D52 , pp. 43-48
    • Cowtan, K.D.1    Main, P.2
  • 24
    • 0001235950 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D., Ten Eyck, L. & Matthews, B. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr. A48, 912-916 (1987).
    • (1987) Acta Crystallogr. , vol.A48 , pp. 912-916
    • Tronrud, D.1    Ten Eyck, L.2    Matthews, B.3
  • 25
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications
    • Brünger, A.T. Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Crystallogr. D49, 24-36 (1993).
    • (1993) Acta Crystallogr. , vol.D49 , pp. 24-36
    • Brünger, A.T.1
  • 26
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • Anderson, B., Baker, H., Morris, G., Rice, D. & Baker, E. Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution. J. Mol. Biol. 209, 711-734 (1989).
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.1    Baker, H.2    Morris, G.3    Rice, D.4    Baker, E.5
  • 27
    • 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. A42, 140-149 (1986).
    • (1986) Acta Crystallogr. , vol.A42 , pp. 140-149
    • Read, R.J.1
  • 28
    • 0027236660 scopus 로고
    • Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution
    • Day, C.L., Anderson, B.F., Tweedie, J.W. & Baker, E.N. Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution. J. Mol. Biol. 232, 1084-1100 (1993).
    • (1993) J. Mol. Biol. , vol.232 , pp. 1084-1100
    • Day, C.L.1    Anderson, B.F.2    Tweedie, J.W.3    Baker, E.N.4
  • 29
    • 0001593248 scopus 로고
    • High-resolution X-ray studies on rabbit serum transferrin. Preliminary structure analysis of the amino-terminal half-molecule at 2.3 Å resolution
    • Sarra, R., Garratt, R., Gorinsky, B., Jhoti, H. & Lindley, P. High-resolution X-ray studies on rabbit serum transferrin. Preliminary structure analysis of the amino-terminal half-molecule at 2.3 Å resolution. Acta Crystallogr. B46, 763-771 (1990).
    • (1990) Acta Crystallogr. , vol.B46 , pp. 763-771
    • Sarra, R.1    Garratt, R.2    Gorinsky, B.3    Jhoti, H.4    Lindley, P.5
  • 30
    • 0000913086 scopus 로고
    • A fast algorithm of rendering space-filling molecule pictures
    • Bacon, D. & Anderson, W. A fast algorithm of rendering space-filling molecule pictures. Journal of Molecular Graphics 6, 219-220 (1988).
    • (1988) Journal of Molecular Graphics , vol.6 , pp. 219-220
    • Bacon, D.1    Anderson, W.2
  • 31
    • 0028057108 scopus 로고
    • Raster3d version 2.0, a program for photorealistic molecular graphics
    • Merritt, E. & Murphy, M. Raster3d version 2.0, a program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.1    Murphy, M.2


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