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Volumn 466, Issue 7309, 2010, Pages 996-1000

Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN FLIG; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; FLIG PROTEIN, BACTERIA; MOLECULAR MOTOR; MOTA PROTEIN, BACTERIA;

EID: 77955924240     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09300     Document Type: Article
Times cited : (155)

References (40)
  • 1
    • 0023128224 scopus 로고
    • Rapid rotation of flagellar bundles in swimming bacteria
    • Lowe, G., Meister, M. & Berg, H. C. Rapid rotation of flagellar bundles in swimming bacteria. Nature 325, 637-640 (1987).
    • (1987) Nature , vol.325 , pp. 637-640
    • Lowe, G.1    Meister, M.2    Berg, H.C.3
  • 2
    • 0027944530 scopus 로고
    • Very fast flagellar rotation
    • Magariyama, Y. et al. Very fast flagellar rotation. Nature 371, 752 (1994).
    • (1994) Nature , vol.371 , pp. 752
    • Magariyama, Y.1
  • 3
    • 0015897650 scopus 로고
    • Bacteria swim by rotating their flagellar filaments
    • Berg, H. C. & Anderson, R. A. Bacteria swim by rotating their flagellar filaments. Nature 245, 380-382 (1973).
    • (1973) Nature , vol.245 , pp. 380-382
    • Berg, H.C.1    Anderson, R.A.2
  • 5
    • 0021037132 scopus 로고
    • 1-driven flagellar motors of an alkalophilic Bacillus strain YN-1
    • 1-driven flagellar motors of an alkalophilic Bacillus strain YN-1. J. Biol. Chem. 258, 10577-10581 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 10577-10581
    • Hirota, N.1    Imae, Y.2
  • 6
    • 0015526205 scopus 로고
    • Chemotaxis in Escherichia coli analysed by three-dimensional tracking
    • Berg, H. C. & Brown, D. A. Chemotaxis in Escherichia coli analysed by three-dimensional tracking. Nature 239, 500-504 (1972).
    • (1972) Nature , vol.239 , pp. 500-504
    • Berg, H.C.1    Brown, D.A.2
  • 7
    • 0034015656 scopus 로고    scopus 로고
    • Real-time imaging of fluorescent flagellar filaments
    • Turner, L., Ryu, W. S. & Berg, H. C. Real-time imaging of fluorescent flagellar filaments. J. Bacteriol. 182, 2793-2801 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 2793-2801
    • Turner, L.1    Ryu, W.S.2    Berg, H.C.3
  • 8
    • 0027407375 scopus 로고
    • Salmonella typhimurium fliG and fliN mutations causing defects in assembly, rotation, and switching of the flagellar motor
    • Irikura, V. M., Kihara, M., Yamaguchi, S., Sockett, H. & Macnab, R. M. Salmonella typhimurium fliG and fliN mutations causing defects in assembly, rotation, and switching of the flagellar motor. J. Bacteriol. 175, 802-810 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 802-810
    • Irikura, V.M.1    Kihara, M.2    Yamaguchi, S.3    Sockett, H.4    MacNab, R.M.5
  • 9
    • 0031557399 scopus 로고    scopus 로고
    • Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli
    • Lloyd, S. A. & Blair, D. F. Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli. J. Mol. Biol. 266, 733-744 (1997).
    • (1997) J. Mol. Biol. , vol.266 , pp. 733-744
    • Lloyd, S.A.1    Blair, D.F.2
  • 10
    • 0030066344 scopus 로고    scopus 로고
    • Torque generation in the flagellar motor of Escherichia coli: Evidence of a direct role for FliG but not for FliM or FliN
    • Lloyd, S. A., Tang, H., Wang, X., Billings, S. & Blair, D. F. Torque generation in the flagellar motor of Escherichia coli: evidence of a direct role for FliG but not for FliM or FliN. J. Bacteriol. 178, 223-231 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 223-231
    • Lloyd, S.A.1    Tang, H.2    Wang, X.3    Billings, S.4    Blair, D.F.5
  • 12
    • 0032568636 scopus 로고    scopus 로고
    • Electrostatic interactions between rotor and stator in the bacterial flagellar motor
    • Zhou, J., Lloyd, S. A. & Blair, D. F. Electrostatic interactions between rotor and stator in the bacterial flagellar motor. Proc. Natl Acad. Sci. USA 95, 6436-6441 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6436-6441
    • Zhou, J.1    Lloyd, S.A.2    Blair, D.F.3
  • 13
    • 0033614958 scopus 로고    scopus 로고
    • Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor
    • Lloyd, S. A., Whitby, F. G., Blair, D. F. & Hill, C. P. Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor. Nature 400, 472-475 (1999).
    • (1999) Nature , vol.400 , pp. 472-475
    • Lloyd, S.A.1    Whitby, F.G.2    Blair, D.F.3    Hill, C.P.4
  • 14
    • 0036646105 scopus 로고    scopus 로고
    • Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG
    • Brown, P. N., Hill, C. P. & Blair, D. F. Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG. EMBO J. 21, 3225-3234 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3225-3234
    • Brown, P.N.1    Hill, C.P.2    Blair, D.F.3
  • 15
    • 0026740392 scopus 로고
    • Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body
    • Francis, N. R., Irikura, V. M., Yamaguchi, S., DeRosier, D. J. & Macnab, R. M. Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body. Proc. Natl Acad. Sci. USA 89, 6304-6308 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6304-6308
    • Francis, N.R.1    Irikura, V.M.2    Yamaguchi, S.3    Derosier, D.J.4    MacNab, R.M.5
  • 16
    • 0026792838 scopus 로고
    • M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF
    • Ueno, T., Oosawa, K. & Aizawa, S. M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF. J. Mol. Biol. 227, 672-677 (1992).
    • (1992) J. Mol. Biol. , vol.227 , pp. 672-677
    • Ueno, T.1    Oosawa, K.2    Aizawa, S.3
  • 17
    • 0034079196 scopus 로고    scopus 로고
    • Deletion analysis of the flagellar switch protein FliG of Salmonella
    • Kihara, M., Miller, G. U. & Macnab, R. M. Deletion analysis of the flagellar switch protein FliG of Salmonella. J. Bacteriol. 182, 3022-3028 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 3022-3028
    • Kihara, M.1    Miller, G.U.2    MacNab, R.M.3
  • 18
    • 0030955083 scopus 로고    scopus 로고
    • An extreme clockwise switch bias mutation in fliG of Salmonella typhimurium and its suppression by slow-motile mutations in motA and motB
    • Togashi, F., Yamaguchi, S., Kihara, M., Aizawa, S. I. & Macnab, R. M. An extreme clockwise switch bias mutation in fliG of Salmonella typhimurium and its suppression by slow-motile mutations in motA and motB. J. Bacteriol. 179, 2994-3003 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 2994-3003
    • Togashi, F.1    Yamaguchi, S.2    Kihara, M.3    Aizawa, S.I.4    MacNab, R.M.5
  • 19
    • 2342607519 scopus 로고    scopus 로고
    • Rusty, jammed, and well-oiled hinges: Mutations affecting the interdomain region of FliG, a rotor element of the Escherichia coli flagellar motor
    • Van Way, S. M., Millas, S. G., Lee, A. H. & Manson, M. D. Rusty, jammed, and well-oiled hinges: mutations affecting the interdomain region of FliG, a rotor element of the Escherichia coli flagellar motor. J. Bacteriol. 186, 3173-3181 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 3173-3181
    • Van Way, S.M.1    Millas, S.G.2    Lee, A.H.3    Manson, M.D.4
  • 21
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin a
    • Conti, E., Uy, M., Leighton, L., Blobel, G. & Kuriyan, J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin a. Cell 94, 193-204 (1998).
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 22
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of b-catenin
    • Huber, A. H., Nelson, W. J. & Weis, W. I. Three-dimensional structure of the armadillo repeat region of b-catenin. Cell 90, 871-882 (1997).
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 23
    • 33846207448 scopus 로고    scopus 로고
    • Mutational analysis of the flagellar protein FliG: Sites of interaction with FliM and implications for organization of the switch complex
    • Brown, P. N., Terrazas, M., Paul, K. & Blair, D. F. Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex. J. Bacteriol. 189, 305-312 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 305-312
    • Brown, P.N.1    Terrazas, M.2    Paul, K.3    Blair, D.F.4
  • 24
    • 0029913699 scopus 로고    scopus 로고
    • A mutational analysis of the interaction between FliG and FliM, two components of the flagellar motor of Escherichia coli
    • Marykwas, D. L. & Berg, H. C. A mutational analysis of the interaction between FliG and FliM, two components of the flagellar motor of Escherichia coli. J.Bacteriol. 178, 1289-1294 (1996).
    • (1996) J.Bacteriol. , vol.178 , pp. 1289-1294
    • Marykwas, D.L.1    Berg, H.C.2
  • 25
    • 33749608423 scopus 로고    scopus 로고
    • The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium
    • Thomas, D. R., Francis, N. R., Xu, C. & DeRosier, D. J. The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium. J. Bacteriol. 188, 7039-7048 (2006).
    • (2006) J. Bacteriol. , vol.188 , pp. 7039-7048
    • Thomas, D.R.1    Francis, N.R.2    Xu, C.3    Derosier, D.J.4
  • 26
    • 0035804929 scopus 로고    scopus 로고
    • Conformational spread in a ring of proteins: A stochastic approach to allostery
    • Duke, T. A., Le Novere, N. & Bray, D. Conformational spread in a ring of proteins: a stochastic approach to allostery. J. Mol. Biol. 308, 541-553 (2001).
    • (2001) J. Mol. Biol. , vol.308 , pp. 541-553
    • Duke, T.A.1    Le Novere, N.2    Bray, D.3
  • 27
    • 76249126819 scopus 로고    scopus 로고
    • Conformational spread as a mechanism for cooperativity in the bacterial flagellar switch
    • Bai, F. et al. Conformational spread as a mechanism for cooperativity in the bacterial flagellar switch. Science 327, 685-689 (2010).
    • (2010) Science , vol.327 , pp. 685-689
    • Bai, F.1
  • 28
    • 0035681962 scopus 로고    scopus 로고
    • Structures of bacterial flagellar motors from two FliF-FliG gene fusion mutants
    • Thomas, D., Morgan, D. G. & DeRosier, D. J. Structures of bacterial flagellar motors from two FliF-FliG gene fusion mutants. J. Bacteriol. 183, 6404-6412 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 6404-6412
    • Thomas, D.1    Morgan, D.G.2    Derosier, D.J.3
  • 29
    • 67749093018 scopus 로고    scopus 로고
    • Intact flagellar motor of Borrelia burgdorferi revealed by cryo-electron tomography: Evidence for stator ring curvature and rotor/C ring assembly flexion
    • Liu, J. et al. Intact flagellar motor of Borrelia burgdorferi revealed by cryo-electron tomography: evidence for stator ring curvature and rotor/C ring assembly flexion. J. Bacteriol. 191, 5026-5036 (2009).
    • (2009) J. Bacteriol. , vol.191 , pp. 5026-5036
    • Liu, J.1
  • 30
    • 33748295677 scopus 로고    scopus 로고
    • In situ structure of the complete Treponema primitia flagellar motor
    • Murphy, G. E., Leadbetter, J. R. & Jensen, G. J. In situ structure of the complete Treponema primitia flagellar motor. Nature 442, 1062-1064 (2006).
    • (2006) Nature , vol.442 , pp. 1062-1064
    • Murphy, G.E.1    Leadbetter, J.R.2    Jensen, G.J.3
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4.. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 33
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy, D. J., Hendrickson, W. A., Aukhil, I. & Erickson, H. P. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258, 987-991 (1992).
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 34
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G. M. A short history of SHELX. Acta Crystallogr. A 64, 112-122 (2008).
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 35
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • Fortelle, E.1    Bricogne, G.2
  • 36
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 37
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 38
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I. W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383 (2007).
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1
  • 39
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky, T. J. et al. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res. 35, W522-W525 (2007).
    • (2007) Nucleic Acids Res. , vol.35
    • Dolinsky, T.J.1


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