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Volumn 6, Issue 7, 1998, Pages 863-874

Crystal structure of a colicin N fragment suggests a model for toxicity

Author keywords

Colicins; Membrane translocation; Porin; Receptor binding; Toxin structure

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0032528046     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00088-4     Document Type: Article
Times cited : (123)

References (73)
  • 1
    • 0028325274 scopus 로고
    • Colicins: Structures, modes of action, transfer through membranes, and evolution
    • Braun, V., Pilsl, H. & Gross, P. (1994). Colicins: structures, modes of action, transfer through membranes, and evolution. Arch. Microbiol. 161, 199-206.
    • (1994) Arch. Microbiol. , vol.161 , pp. 199-206
    • Braun, V.1    Pilsl, H.2    Gross, P.3
  • 2
    • 0028331315 scopus 로고
    • All in the family: The toxic activity of pore-forming colicins
    • Lakey, J.H., van der Goot, F.G. & Pattus, F. (1994). All in the family: the toxic activity of pore-forming colicins. Toxicology 87, 85-108.
    • (1994) Toxicology , vol.87 , pp. 85-108
    • Lakey, J.H.1    Van Der Goot, F.G.2    Pattus, F.3
  • 4
    • 0011532359 scopus 로고    scopus 로고
    • Insights into membrane insertion based on studies of colicins
    • (Parker, M.W., ed.) R.G. Landes Company, Austin, Texas
    • Vetter, I.R., Parker, M.W., Pattus, F. & Tsernoglou, D.T. (1996). Insights into membrane insertion based on studies of colicins. In Protein Toxin Structure. (Parker, M.W., ed.), pp. 5-23, R.G. Landes Company, Austin, Texas.
    • (1996) Protein Toxin Structure , pp. 5-23
    • Vetter, I.R.1    Parker, M.W.2    Pattus, F.3    Tsernoglou, D.T.4
  • 5
    • 0031569404 scopus 로고    scopus 로고
    • The long and short of colicin action - The molecular basis for the biological activity of channel-forming colicins
    • Gouaux, E. (1997). The long and short of colicin action - the molecular basis for the biological activity of channel-forming colicins. Structure 5, 313-317.
    • (1997) Structure , vol.5 , pp. 313-317
    • Gouaux, E.1
  • 6
    • 0024452245 scopus 로고
    • The structurally related exbB and tolQ genes are interchangeable in conferring tonB-dependent colicin, bacteriophage, and albomycin sensitivity
    • Braun, V. (1989). The structurally related exbB and tolQ genes are interchangeable in conferring tonB-dependent colicin, bacteriophage, and albomycin sensitivity. J. Bacteriol. 171, 6387-6390.
    • (1989) J. Bacteriol. , vol.171 , pp. 6387-6390
    • Braun, V.1
  • 7
    • 0027752437 scopus 로고
    • TonB protein and energy transduction between membranes
    • Postle, K. (1993). TonB protein and energy transduction between membranes. J. Bioenerg. Biomembr. 25, 591-601.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 591-601
    • Postle, K.1
  • 8
    • 0025897173 scopus 로고
    • The toi gene products and the import of macromolecules into Escherichia coli
    • Webster, R.E. (1991). The toi gene products and the import of macromolecules into Escherichia coli. Mol. Microbiol. 5, 1005-1011.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1005-1011
    • Webster, R.E.1
  • 9
    • 8944230187 scopus 로고    scopus 로고
    • Characterization of the tol/pal region of E. coli K12
    • Vianney, A., et al., & Webster, R.E. (1996). Characterization of the tol/pal region of E. coli K12. J. Bacteriol. 178, 4031-4038.
    • (1996) J. Bacteriol. , vol.178 , pp. 4031-4038
    • Vianney, A.1    Webster, R.E.2
  • 10
    • 0024789570 scopus 로고
    • Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli
    • Bénédetti, H., et al., & Lazdunski, C. (1989). Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli. J. Gen. Microbiol. 135, 3413-3420.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 3413-3420
    • Bénédetti, H.1    Lazdunski, C.2
  • 11
    • 0030944701 scopus 로고    scopus 로고
    • The ToIA protein interacts with colicin E1 differently than with other group A colicins
    • Schendel, S.L., Click, E.M., Webster, R.E. & Cramer, W.A. (1997). The ToIA protein interacts with colicin E1 differently than with other group A colicins. J. Bacteriol. 179, 3683-3690.
    • (1997) J. Bacteriol. , vol.179 , pp. 3683-3690
    • Schendel, S.L.1    Click, E.M.2    Webster, R.E.3    Cramer, W.A.4
  • 12
    • 0031034934 scopus 로고    scopus 로고
    • The N-terminal domain of colicin E3 interacts with Tolb which is involved in the colicin translocation step
    • Bouveret, E., Rigal, A., Lazdunski, C. & Benedetti, H. (1997). The N-terminal domain of colicin E3 interacts with Tolb which is involved in the colicin translocation step. Mol. Microbiol. 23, 909-920.
    • (1997) Mol. Microbiol. , vol.23 , pp. 909-920
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Benedetti, H.4
  • 13
    • 0021966775 scopus 로고
    • Escherichia coli K1 2 strains for use in the identification and characterization of colicins
    • Pugsley, A.P. (1985). Escherichia coli K1 2 strains for use in the identification and characterization of colicins. J. Gen. Microbiol. 131, 369-376.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 369-376
    • Pugsley, A.P.1
  • 14
    • 0028905676 scopus 로고
    • Novel colicin 10: Assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation
    • Pilsl, H. & Braun, V. (1995). Novel colicin 10: assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation. Mol. Microbiol. 16, 57-67.
    • (1995) Mol. Microbiol. , vol.16 , pp. 57-67
    • Pilsl, H.1    Braun, V.2
  • 15
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: Consensus pentapeptide among TonB-dependent colicins and receptors
    • Schramm, E., Mende, J., Braun, V. & Kamp, R.M. (1987). Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors. J. Bacteriol. 169, 3350-3357.
    • (1987) J. Bacteriol. , vol.169 , pp. 3350-3357
    • Schramm, E.1    Mende, J.2    Braun, V.3    Kamp, R.M.4
  • 16
    • 0019967083 scopus 로고
    • Effects of bacteriophage f1 gene III protein on the host cell membrane
    • Boeke, J.D., Model, P. & Zinder, N.D. (1982). Effects of bacteriophage f1 gene III protein on the host cell membrane. Mol. Gen. Genet. 186, 185-192.
    • (1982) Mol. Gen. Genet. , vol.186 , pp. 185-192
    • Boeke, J.D.1    Model, P.2    Zinder, N.D.3
  • 17
    • 0025049224 scopus 로고
    • Import-defective colicin B derivatives mutated in the TonB box
    • Mende, J. & Braun, V. (1990). Import-defective colicin B derivatives mutated in the TonB box. Mol. Microbiol. 4, 1523-1533.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1523-1533
    • Mende, J.1    Braun, V.2
  • 18
    • 0027202188 scopus 로고
    • Phosphate efflux through the channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP
    • Guihard, G., Bénédetti, H., Besnard, M. & Letellier, L. (1993). Phosphate efflux through the channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP. J. Biol. Chem. 268, 17775-17780.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17775-17780
    • Guihard, G.1    Bénédetti, H.2    Besnard, M.3    Letellier, L.4
  • 19
    • 0018236743 scopus 로고
    • Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes
    • Schein, SJ., Kagan, B.L. & Finkelstein, A. (1978). Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes. Nature 276, 159-163.
    • (1978) Nature , vol.276 , pp. 159-163
    • Schein, S.J.1    Kagan, B.L.2    Finkelstein, A.3
  • 20
    • 0021092930 scopus 로고
    • Isolation, molecular and functional properties of the C-terminal domain of colicin A
    • Martinez, M.C., Lazdunski, C. & Pattus, F. (1983). Isolation, molecular and functional properties of the C-terminal domain of colicin A. EMBO J. 2, 1501-1507.
    • (1983) EMBO J. , vol.2 , pp. 1501-1507
    • Martinez, M.C.1    Lazdunski, C.2    Pattus, F.3
  • 21
    • 0023791146 scopus 로고
    • Colicin E1 in planar lipid bilayers
    • Slatin, S.L. (1988). Colicin E1 in planar lipid bilayers. Int. J. Biochem. 20, 737-744.
    • (1988) Int. J. Biochem. , vol.20 , pp. 737-744
    • Slatin, S.L.1
  • 22
    • 0025289717 scopus 로고
    • Colicin N forms voltage- and pH-dependent channels in planar lipid bilayer membranes
    • Wilmsen, H.U., Pugsley, A.P. & Pattus, F. (1990). Colicin N forms voltage- and pH-dependent channels in planar lipid bilayer membranes. Eur. Biophys. J. 18, 149-158.
    • (1990) Eur. Biophys. J. , vol.18 , pp. 149-158
    • Wilmsen, H.U.1    Pugsley, A.P.2    Pattus, F.3
  • 23
    • 0027336342 scopus 로고
    • A carboxy-terminal fragment of colicin la forms ion channels
    • Ghosh, P., Mel, S.F. & Stroud, R.M. (1993). A carboxy-terminal fragment of colicin la forms ion channels. J. Membr. Biol. 134, 85-92.
    • (1993) J. Membr. Biol. , vol.134 , pp. 85-92
    • Ghosh, P.1    Mel, S.F.2    Stroud, R.M.3
  • 24
    • 0024961641 scopus 로고
    • Structure of the membrane-pore-forming fragment of colicin A
    • Parker, M.W., Pattus, F., Tucker, A.D. & Tsernoglou, D. (1989). Structure of the membrane-pore-forming fragment of colicin A. Nature 337, 93-96.
    • (1989) Nature , vol.337 , pp. 93-96
    • Parker, M.W.1    Pattus, F.2    Tucker, A.D.3    Tsernoglou, D.4
  • 25
    • 0031569354 scopus 로고    scopus 로고
    • A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1
    • Elkins, P., Bunker, A., Cramer, W.A. & Stauffacher, C.V. (1997). A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1. Structure 5, 443-458.
    • (1997) Structure , vol.5 , pp. 443-458
    • Elkins, P.1    Bunker, A.2    Cramer, W.A.3    Stauffacher, C.V.4
  • 27
    • 0025932041 scopus 로고
    • A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
    • van der Goot, F.G., Gonzalez-Mañas, J.M., Lakey, J.H. & Pattus, F. (1991). A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A. Nature 354, 408-410.
    • (1991) Nature , vol.354 , pp. 408-410
    • Van Der Goot, F.G.1    Gonzalez-Mañas, J.M.2    Lakey, J.H.3    Pattus, F.4
  • 28
    • 0027328666 scopus 로고
    • Acrylamide quenching of the intrinsic fluorescence of tryptophan residues genetically engineered into the soluble colicin E1 channel peptide. Structural characterization of the insertion-competent state
    • Merrill, A.R., Palmer, L.R. & Szabo, A.G. (1993). Acrylamide quenching of the intrinsic fluorescence of tryptophan residues genetically engineered into the soluble colicin E1 channel peptide. Structural characterization of the insertion-competent state. Biochemistry 32, 6974-6981.
    • (1993) Biochemistry , vol.32 , pp. 6974-6981
    • Merrill, A.R.1    Palmer, L.R.2    Szabo, A.G.3
  • 29
    • 0027157448 scopus 로고
    • Fluorescence energy transfer distance measurements. The hydrophobic helical hairpin of colicin A in the membrane bound state
    • Lakey, J.H., Duche, D., Gonzalez-Mañas, J.M., Baty, D. & Pattus, F. (1993). Fluorescence energy transfer distance measurements. The hydrophobic helical hairpin of colicin A in the membrane bound state. J. Mol. Biol. 230, 1055-1067.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1055-1067
    • Lakey, J.H.1    Duche, D.2    Gonzalez-Mañas, J.M.3    Baty, D.4    Pattus, F.5
  • 30
    • 0027447891 scopus 로고
    • Colicin E1 binding to membranes: Time-resolved studies of spin-labeled mutants
    • Shin, Y.K., Levinthal, C., Levinthal, F. & Hubbell, W.L (1993). Colicin E1 binding to membranes: time-resolved studies of spin-labeled mutants. Science 259, 960-963.
    • (1993) Science , vol.259 , pp. 960-963
    • Shin, Y.K.1    Levinthal, C.2    Levinthal, F.3    Hubbell, W.L.4
  • 31
    • 0029848960 scopus 로고    scopus 로고
    • Different sensitivities to acid denaturation within a family of proteins - Implications for acid unfolding and membrane translocation
    • Evans, L., Goble, M.L, Hales, K.A. & Lakey, J.H. (1996). Different sensitivities to acid denaturation within a family of proteins - implications for acid unfolding and membrane translocation. Biochemistry 35, 13180-13185.
    • (1996) Biochemistry , vol.35 , pp. 13180-13185
    • Evans, L.1    Goble, M.L.2    Hales, K.A.3    Lakey, J.H.4
  • 33
    • 0028100898 scopus 로고
    • Identification of a translocated protein segment in a voltage-dependent channel
    • Slatin, S.L., Qiu, X.Q., Jakes, K.S. & Finkelstein, A. (1994). Identification of a translocated protein segment in a voltage-dependent channel. Nature 371, 960-963.
    • (1994) Nature , vol.371 , pp. 960-963
    • Slatin, S.L.1    Qiu, X.Q.2    Jakes, K.S.3    Finkelstein, A.4
  • 35
    • 0026541379 scopus 로고
    • Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed
    • Bénédetti, H., Lloubès, R., Lazdunski, C. & Letellier, C. (1992). Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed. EMBO J. 11, 441-447.
    • (1992) EMBO J. , vol.11 , pp. 441-447
    • Bénédetti, H.1    Lloubès, R.2    Lazdunski, C.3    Letellier, C.4
  • 36
    • 0027938907 scopus 로고
    • Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering
    • Duché, D., Baty, D., Chartier, M. & Letellier, L (1994). Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering. J. Biol. Chem. 269, 24820-24825.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24820-24825
    • Duché, D.1    Baty, D.2    Chartier, M.3    Letellier, L.4
  • 37
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E. coli porins
    • Cowan, S.W., et al., & Rosenbusch, J.P. (1992). Crystal structures explain functional properties of two E. coli porins. Nature 358, 727-733.
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Rosenbusch, J.P.2
  • 38
    • 0027459747 scopus 로고
    • Structural alignment of globins, phycocyanins and colicin A
    • Holm L. & Sander C. (1993). Structural alignment of globins, phycocyanins and colicin A. FEBS Lett. 315, 301-306.
    • (1993) FEBS Lett. , vol.315 , pp. 301-306
    • Holm, L.1    Sander, C.2
  • 39
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm L. & Sander C. (1994). The FSSP database of structurally aligned protein fold families. Nucleic Acids Res. 22, 3600-3609.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 40
    • 1842332735 scopus 로고    scopus 로고
    • Bcl-xL forms an ion channel in synthetic lipid membranes
    • Minn, A.J., et al., & Thompson, C.B. (1997). Bcl-xL forms an ion channel in synthetic lipid membranes. Nature 385, 353-357.
    • (1997) Nature , vol.385 , pp. 353-357
    • Minn, A.J.1    Thompson, C.B.2
  • 41
    • 0026581661 scopus 로고
    • Refined structure of the pore-forming domain of colicin A at 2.4 Å resolution
    • Parker, M.W., Postma, J.P.M., Pattus, F., Tucker, A.D. & Tsernoglou, D. (1992). Refined structure of the pore-forming domain of colicin A at 2.4 Å resolution. J. mol. Biol. 224, 639-657.
    • (1992) J. Mol. Biol. , vol.224 , pp. 639-657
    • Parker, M.W.1    Postma, J.P.M.2    Pattus, F.3    Tucker, A.D.4    Tsernoglou, D.5
  • 42
    • 0024066065 scopus 로고
    • The 2.0 ÀX-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W., et al., & Turk, V. (1988). The 2.0 ÀX-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7, 2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Turk, V.2
  • 43
    • 0028829320 scopus 로고
    • Structure of the fibre-forming protein pilin at 2.6 A resolution
    • Parge, H.E., et al., & Tainer, J.A. (1995). Structure of the fibre-forming protein pilin at 2.6 A resolution. Nature 378, 32-38.
    • (1995) Nature , vol.378 , pp. 32-38
    • Parge, H.E.1    Tainer, J.A.2
  • 44
    • 0027223073 scopus 로고
    • Characterization of the receptor and translocation domains of colicin N
    • El Kouhen, R., et al., & Pages, J-M. (1993). Characterization of the receptor and translocation domains of colicin N. Eur. J. Biochem. 214, 635-639.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 635-639
    • El Kouhen, R.1    Pages, J.-M.2
  • 45
    • 0031799096 scopus 로고    scopus 로고
    • Discovery of critical TolA-binding residues in the bactericidal toxin colicin N: A biophysical approach
    • in press
    • Raggett, E.M., Bainbridge, G., Evans, L.J.A., Cooper, A. & Lakey, J.H. (1998). Discovery of critical TolA-binding residues in the bactericidal toxin colicin N: a biophysical approach. Mol. Microbiol., in press.
    • (1998) Mol. Microbiol.
    • Raggett, E.M.1    Bainbridge, G.2    Evans, L.J.A.3    Cooper, A.4    Lakey, J.H.5
  • 46
    • 0029857393 scopus 로고    scopus 로고
    • The central domain of colicin N possesses the receptor recognition site but not the binding affinity of the whole toxin
    • Evans, L.J.A., Labeit, S., Cooper, A., Bond, L.H. & Lakey, J.H. (1996). The central domain of colicin N possesses the receptor recognition site but not the binding affinity of the whole toxin. Biochemistry 35, 15143-15148.
    • (1996) Biochemistry , vol.35 , pp. 15143-15148
    • Evans, L.J.A.1    Labeit, S.2    Cooper, A.3    Bond, L.H.4    Lakey, J.H.5
  • 47
    • 0029151113 scopus 로고
    • Colicin import and pore formation: A system for studying protein transport across membranes?
    • Lazdunski, C. (1995). Colicin import and pore formation: a system for studying protein transport across membranes? Mol. Microbiol. 16, 1059-1066.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1059-1066
    • Lazdunski, C.1
  • 48
    • 0025237625 scopus 로고
    • Uptake across the cell envelope and insertion into the inner membrane of ion channel-forming colicins in E. coli
    • Baty, D., et al., & Lazdunski, C. (1990). Uptake across the cell envelope and insertion into the inner membrane of ion channel-forming colicins in E. coli. Biochimie 72, 123-130.
    • (1990) Biochimie , vol.72 , pp. 123-130
    • Baty, D.1    Lazdunski, C.2
  • 49
    • 0021738087 scopus 로고
    • Gene encoding a hybrid OmpF-PhoE pore protein in the outer membrane of Escherichia coli K12
    • Tommassen, J., Pugsley, A.P., Korteland, J., Verbakel, J. & Lugtenberg, B. (1984). Gene encoding a hybrid OmpF-PhoE pore protein in the outer membrane of Escherichia coli K12. Mol. Gen. Genet. 197, 503-508.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 503-508
    • Tommassen, J.1    Pugsley, A.P.2    Korteland, J.3    Verbakel, J.4    Lugtenberg, B.5
  • 50
    • 0025114009 scopus 로고
    • Involvement of OmpF during reception and translocation steps of colicin N entry
    • Bourdineaud, J.-P., Fierobe, H.P., Lazdunski, C. & Pagès, J.M. (1990). Involvement of OmpF during reception and translocation steps of colicin N entry. Mol. Microbiol. 4, 1737-1743.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1737-1743
    • Bourdineaud, J.-P.1    Fierobe, H.P.2    Lazdunski, C.3    Pagès, J.M.4
  • 51
    • 0029963892 scopus 로고    scopus 로고
    • Direct measurement of the association of a protein with a family of membrane receptors
    • Evans, L.J.A., Cooper, A. & Lakey, J.H. (1996). Direct measurement of the association of a protein with a family of membrane receptors. J. Mol. Biol. 255, 559-563.
    • (1996) J. Mol. Biol. , vol.255 , pp. 559-563
    • Evans, L.J.A.1    Cooper, A.2    Lakey, J.H.3
  • 52
    • 0025300119 scopus 로고
    • Characterization of OmpF domains involved in Escherichia coli K-12 sensitivity to colicins A and N
    • Fourel, D., Hikita, C., Bella, J.-M., Mizushima, S. & Pagès, J.-M. (1990). Characterization of OmpF domains involved in Escherichia coli K-12 sensitivity to colicins A and N. J. Bacteriol. 172, 3675-3680.
    • (1990) J. Bacteriol. , vol.172 , pp. 3675-3680
    • Fourel, D.1    Hikita, C.2    Bella, J.-M.3    Mizushima, S.4    Pagès, J.-M.5
  • 53
    • 0027152155 scopus 로고
    • Specific regions of Escherichia coli OmpF protein involved in antigenic and colicin receptor sites and in stable trimerization
    • Fourel, D., Mizushima, S., Bernadac, A. & Pagès, J.-M. (1993). Specific regions of Escherichia coli OmpF protein involved in antigenic and colicin receptor sites and in stable trimerization. J. Bacteriol. 175, 2754-2757.
    • (1993) J. Bacteriol. , vol.175 , pp. 2754-2757
    • Fourel, D.1    Mizushima, S.2    Bernadac, A.3    Pagès, J.-M.4
  • 54
    • 0029811916 scopus 로고    scopus 로고
    • Dynamic aspects of colicin N translocation through the Escherichia coli outer membrane
    • El Kouhen, R. & Pagès, J.-M. (1996). Dynamic aspects of colicin N translocation through the Escherichia coli outer membrane. J. Bacteriol. 178, 5316-5319.
    • (1996) J. Bacteriol. , vol.178 , pp. 5316-5319
    • El Kouhen, R.1    Pagès, J.-M.2
  • 55
    • 0027970976 scopus 로고
    • Structural and functional alterations of a colicin-resistant mutant of OmpF-porin from Escherichia coli
    • Jeanteur, D., et al., & Pagès, J.M. (1994). Structural and functional alterations of a colicin-resistant mutant of OmpF-porin from Escherichia coli. Proc. Natl Acad. Sci. USA 91, 10675-10679.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10675-10679
    • Jeanteur, D.1    Pagès, J.M.2
  • 56
    • 0025915509 scopus 로고
    • Protein import into Escherichia coli: Colicins A and E1 interact with a component of their translocation system
    • Bénédetti, H., Lazdunski, C. & Lloubès, R. (1991). Protein import into Escherichia coli: colicins A and E1 interact with a component of their translocation system. EMBO J. 10, 1989-1995.
    • (1991) EMBO J. , vol.10 , pp. 1989-1995
    • Bénédetti, H.1    Lazdunski, C.2    Lloubès, R.3
  • 57
    • 0028339520 scopus 로고
    • Involvement of exposed loops for the trimeric stability and for membrane insertion of the Escherichia coli OmpF porin
    • Fourel, D., Bernadac, A. & Pagès, J.M. (1994). Involvement of exposed loops for the trimeric stability and for membrane insertion of the Escherichia coli OmpF porin. Eur. J. Biochem. 222, 625-630.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 625-630
    • Fourel, D.1    Bernadac, A.2    Pagès, J.M.3
  • 58
    • 0030001018 scopus 로고    scopus 로고
    • Membrane topology of the colicin A pore-forming domain analyzed by disulfide bond engineering
    • Duché, D., et al., & Baty, D. (1996). Membrane topology of the colicin A pore-forming domain analyzed by disulfide bond engineering. J. Biol. Chem. 271, 15401-15406.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15401-15406
    • Duché, D.1    Baty, D.2
  • 59
    • 0025253337 scopus 로고
    • A 136 amino acid residue COOH-terminal fragment of colicin A is endowed with ionophoric activity
    • Baty, D., Lakey, J., Pattus, F. & Lazdunski, C. (1990). A 136 amino acid residue COOH-terminal fragment of colicin A is endowed with ionophoric activity. Eur. J. Biochem. 189, 409-413.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 409-413
    • Baty, D.1    Lakey, J.2    Pattus, F.3    Lazdunski, C.4
  • 60
    • 0024817470 scopus 로고
    • Colicin N and its thermolytic fragment induce phospholipid vesicle fusion
    • Massotte, D. & Pattus, F. (1989). Colicin N and its thermolytic fragment induce phospholipid vesicle fusion. FEBS Lett. 257, 447-450.
    • (1989) FEBS Lett. , vol.257 , pp. 447-450
    • Massotte, D.1    Pattus, F.2
  • 61
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 62
    • 85046526624 scopus 로고
    • Evaluation of single crystal X-ray diffraction data from a photon sensitive detector
    • Kabsch, W. (1988). Evaluation of single crystal X-ray diffraction data from a photon sensitive detector. J. Appl. Crystallogr. 21, 916-924.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 63
    • 84945110538 scopus 로고
    • Methodology employed for the structure determination of tumour necrosis factor, a case of high non-crystallographic symmetry
    • Jones, E.Y., Walker, N.P.C. & Stuart, D.I. (1991). Methodology employed for the structure determination of tumour necrosis factor, a case of high non-crystallographic symmetry. Acta Crystallogr. A 47, 753-770.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 753-770
    • Jones, E.Y.1    Walker, N.P.C.2    Stuart, D.I.3
  • 64
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of error in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of error in these models. Acta Crystallogr. A 42, 110-119.
    • (1991) Acta Crystallogr. A , vol.42 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 65
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 67
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F. & Matthews, B.W. (1987). An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr. A 43, 489-501.
    • (1987) Acta Crystallogr. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 69
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy, R., Bowie, J.U. & Eisenberg, D. (1992). Assessment of protein models with three-dimensional profiles. Nature 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 70
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 71
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-293.
    • (1991) Proteins , vol.11 , pp. 281-293
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 72
    • 33845377446 scopus 로고
    • Computation of molecular volume
    • Connolly, M.L. (1985). Computation of molecular volume. J. Am. Chem. Soc. 107, 1118-1124.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 1118-1124
    • Connolly, M.L.1
  • 73
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997). An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graphics 15, 132-134.
    • (1997) J. Mol. Graphics , vol.15 , pp. 132-134
    • Esnouf, R.M.1


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