메뉴 건너뛰기




Volumn 391, Issue 6663, 1998, Pages 203-206

Crystal structure of the bacterial cell-division protein FtsZ

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GUANOSINE TRIPHOSPHATASE;

EID: 2642593025     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/34472     Document Type: Article
Times cited : (742)

References (30)
  • 1
    • 0030901357 scopus 로고    scopus 로고
    • Bacterial cell division: The cycle of the ring
    • Rothfield, L. I. & Justice, S. S. Bacterial cell division: the cycle of the ring. Cell 88, 581-584 (1997).
    • (1997) Cell , vol.88 , pp. 581-584
    • Rothfield, L.I.1    Justice, S.S.2
  • 2
    • 0027460891 scopus 로고
    • The cell cycle of Escherichia coli
    • Donachie, W. D. The cell cycle of Escherichia coli. Annu. Rev. Microbiol. 47, 199-230 (1993).
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 199-230
    • Donachie, W.D.1
  • 3
    • 0030829601 scopus 로고    scopus 로고
    • FtsZ, a tubulin homologue, in prokaryote cell division
    • Erickson, H. P. FtsZ, a tubulin homologue, in prokaryote cell division. Trends Cell Biol. 7, 362-367 (1997).
    • (1997) Trends Cell Biol. , vol.7 , pp. 362-367
    • Erickson, H.P.1
  • 4
    • 0027184918 scopus 로고
    • FtsZ ring in bacterial cytokinesis
    • Lutkenhaus, J. FtsZ ring in bacterial cytokinesis. Mol. Microbiol. 9, 403-409 (1993).
    • (1993) Mol. Microbiol. , vol.9 , pp. 403-409
    • Lutkenhaus, J.1
  • 5
    • 0026705484 scopus 로고
    • The essential bacterial cell-division protein FtsZ is a GTPase
    • de Boer, P., Crossley, R. & Rothfield, L. The essential bacterial cell-division protein FtsZ is a GTPase. Nature 359, 254-256 (1992).
    • (1992) Nature , vol.359 , pp. 254-256
    • De Boer, P.1    Crossley, R.2    Rothfield, L.3
  • 6
    • 0026778964 scopus 로고
    • Escherichia coli cell-division gene FtsZ encodes a novel GTP-binding protein
    • RayChaudhuri, D. & Park, J. T. Escherichia coli cell-division gene FtsZ encodes a novel GTP-binding protein. Nature 359, 251-254 (1992).
    • (1992) Nature , vol.359 , pp. 251-254
    • RayChaudhuri, D.1    Park, J.T.2
  • 7
    • 0028872562 scopus 로고
    • FtsZ, a prokaryotic homolog of tubulin?
    • Erickson, H. P. FtsZ, a prokaryotic homolog of tubulin? Cell 80, 367-370 (1995).
    • (1995) Cell , vol.80 , pp. 367-370
    • Erickson, H.P.1
  • 8
    • 0028290692 scopus 로고
    • GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules
    • Bramhill, D. & Thompson, C. M. GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules. Proc. Natl Acad. Sci. USA 91, 5813-5817 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5813-5817
    • Bramhill, D.1    Thompson, C.M.2
  • 9
    • 0028274791 scopus 로고
    • Guanine nucleotide-dependent assembly of FtsZ into filaments
    • Mukherjee, A. & Lutkenhaus, J. Guanine nucleotide-dependent assembly of FtsZ into filaments. J. Bacteriol. 176, 2754-2758 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 2754-2758
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 10
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S. G. & Downing, K. H. Structure of the αβ tubulin dimer by electron crystallography. Nature 391, 199-203 (1998).
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 11
    • 0344189130 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult, C. J. et al. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 269, 496-512 (1996).
    • (1996) Science , vol.269 , pp. 496-512
    • Bult, C.J.1
  • 12
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B. & Walker, J. E. Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298 (1996).
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 13
    • 0026086679 scopus 로고
    • Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP
    • Tong, L., de Vos, A. M., Milburn, M. V. & Kim, S.-H. Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J. Mol. Biol. 217, 503-513 (1991).
    • (1991) J. Mol. Biol. , vol.217 , pp. 503-513
    • Tong, L.1    De Vos, A.M.2    Milburn, M.V.3    Kim, S.-H.4
  • 14
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • Rossmann, M. G., Moras, D. & Olsen, K. Chemical and biological evolution of a nucleotide-binding protein. Nature 250, 194-199 (1974).
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.3
  • 15
    • 0027992458 scopus 로고
    • The monofunctional chorismate mutase from Bacillus subtilis: Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications on the mechanism of enzymatic reaction
    • Chook, Y. M., Gray, J. V., Ke, H. & Lipscomb, W. N. The monofunctional chorismate mutase from Bacillus subtilis: structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications on the mechanism of enzymatic reaction. J. Mol. Biol. 240, 476-500 (1994).
    • (1994) J. Mol. Biol. , vol.240 , pp. 476-500
    • Chook, Y.M.1    Gray, J.V.2    Ke, H.3    Lipscomb, W.N.4
  • 16
    • 0023754156 scopus 로고
    • The GTP-binding peptide of β-tubulin
    • Linse, K. & Mandelkow, E.-M. The GTP-binding peptide of β-tubulin. J. Biol. Chem. 263, 15205-15210 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 15205-15210
    • Linse, K.1    Mandelkow, E.-M.2
  • 17
    • 0029652724 scopus 로고
    • Site-directed mutagenesis of putative GTP-binding sites of yeast β-tubulin: Evidence that α-, β- And γ-tubulins are atypical GTPases
    • Sage, C. R. et al. Site-directed mutagenesis of putative GTP-binding sites of yeast β-tubulin: evidence that α-, β-and γ-tubulins are atypical GTPases. Biochemistry 34, 16870-16875 (1995).
    • (1995) Biochemistry , vol.34 , pp. 16870-16875
    • Sage, C.R.1
  • 18
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., Sanders, D. A. & McCormick, F. The GTPase superfamily: conserved structure and molecular mechanism. Narure 349, 117-127 (1991).
    • (1991) Narure , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 19
    • 0027500054 scopus 로고
    • Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein
    • Mukherjee, A., Dai, K. & Lutkenhaus, J. Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein. Proc. Natl Acad. Sci. USA 90, 1053-1057 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1053-1057
    • Mukherjee, A.1    Dai, K.2    Lutkenhaus, J.3
  • 20
    • 0029852223 scopus 로고    scopus 로고
    • Tubulin secondary structure analysis, limited proteolysis sites, and homology to FtsZ
    • de Pereda, J. M., Leynadier, D., Evangelio, J. A., Chacon, P. & Andreu, J. M. Tubulin secondary structure analysis, limited proteolysis sites, and homology to FtsZ. Biochemistry 35, 14203-14215 (1996).
    • (1996) Biochemistry , vol.35 , pp. 14203-14215
    • De Pereda, J.M.1    Leynadier, D.2    Evangelio, J.A.3    Chacon, P.4    Andreu, J.M.5
  • 21
    • 0029190887 scopus 로고
    • Structure and function in the tubulin dimer and the role of the acidic carboxyl terminus
    • Sackett, D. L. Structure and function in the tubulin dimer and the role of the acidic carboxyl terminus. Subcell. Biochem. 24, 255-302 (1995).
    • (1995) Subcell. Biochem. , vol.24 , pp. 255-302
    • Sackett, D.L.1
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 54, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.54 , pp. 760-763
  • 25
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1-ATPase
    • Abrahams, J. P. & Leslie, A. G. W. Methods used in the structure determination of bovine mitochondrial F1-ATPase. Acta Crystallogr. D 52, 30-42 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 26
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, T. A. A graphics model building and refinement system for macromolecules. J. Appl. Cryst. 11, 268-272 (1978).
    • (1978) J. Appl. Cryst. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950 (1991).
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 30
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G. J. ALSCRIPT: a tool to format multiple sequence alignments. Prot. Eng. 6, 37-40 (1993).
    • (1993) Prot. Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.