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Volumn 76, Issue 2, 1999, Pages 837-845

Genetically engineered metal ion binding sites on the outside of a channel's transmembrane β-barrel

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID DERIVATIVE; COBALT; COPPER; HEMOLYSIN; HISTIDINE DERIVATIVE; ION CHANNEL; METAL ION; NICKEL; ZINC;

EID: 0032987931     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77247-4     Document Type: Article
Times cited : (77)

References (41)
  • 1
    • 0028809730 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α-subunit
    • Akabas, M. H., and A. Karlin. 1992. Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α-subunit. Biochemistry: 34:12496-12500.
    • (1992) Biochemistry , vol.34 , pp. 12496-12500
    • Akabas, M.H.1    Karlin, A.2
  • 2
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M. H., D. A. Stauffer, M. Xu, and A. Karlin. 1992. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science. 258:307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 3
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach, C., T. Marti, H. G. Khorana, and W. L. Hubbell. 1990. Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science. 248:1088-1092.
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 4
    • 0025730892 scopus 로고
    • Engineered metal-binding proteins: Purification to protein folding
    • Arnold, F. H., and B. L. Haymore. 1991. Engineered metal-binding proteins: purification to protein folding. Science. 252:1796-1797.
    • (1991) Science , vol.252 , pp. 1796-1797
    • Arnold, F.H.1    Haymore, B.L.2
  • 5
    • 0026755899 scopus 로고
    • Molecular localization of an ion-binding site within the pore of mammalian sodium channels
    • Backx, P. H., D. T. Yue, J. H. Lawrence, E. Marban, and G. Tomaselli. 1992. Molecular localization of an ion-binding site within the pore of mammalian sodium channels. Science. 257:248-251.
    • (1992) Science , vol.257 , pp. 248-251
    • Backx, P.H.1    Yue, D.T.2    Lawrence, J.H.3    Marban, E.4    Tomaselli, G.5
  • 6
    • 0030024628 scopus 로고    scopus 로고
    • Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling
    • Barranger-Mathys, M., and D. S. Cafiso. 1996. Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling. Biochemistry. 35:498-505.
    • (1996) Biochemistry , vol.35 , pp. 498-505
    • Barranger-Mathys, M.1    Cafiso, D.S.2
  • 7
    • 0000067560 scopus 로고
    • Current noise reveals protonation kinetics and number of ionizable sites in an open protein ion channel
    • Bezrukov, S. M., and J. J. Kasianowicz. 1993. Current noise reveals protonation kinetics and number of ionizable sites in an open protein ion channel. Phys. Rev. Lett. 70:2352-2355.
    • (1993) Phys. Rev. Lett. , vol.70 , pp. 2352-2355
    • Bezrukov, S.M.1    Kasianowicz, J.J.2
  • 8
    • 0030710585 scopus 로고    scopus 로고
    • Charge state of an ion channel controls neutral polymer entry into its pore
    • Bezrukov, S. M., and J. J. Kasianowicz. 1997. Charge state of an ion channel controls neutral polymer entry into its pore. Eur. Biophys. J. 6:471-476.
    • (1997) Eur. Biophys. J. , vol.6 , pp. 471-476
    • Bezrukov, S.M.1    Kasianowicz, J.J.2
  • 9
    • 0030384264 scopus 로고    scopus 로고
    • Dynamics and free energy of polymers partitioning into a nanoscale pore
    • Bezrukov, S. M., I. Vodyanoy, R. A. Brutyan, and J. J. Kasianowicz. 1996. Dynamics and free energy of polymers partitioning into a nanoscale pore. Macromolecules. 29:8517-8522.
    • (1996) Macromolecules , vol.29 , pp. 8517-8522
    • Bezrukov, S.M.1    Vodyanoy, I.2    Brutyan, R.A.3    Kasianowicz, J.J.4
  • 11
    • 0031404458 scopus 로고    scopus 로고
    • Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β-barrel
    • Cheley, S., M. S. Malghani, L. Song, M. Hobaugh, J. E. Gouaux, J. Yang, and H. Bayley. 1997. Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β-barrel. Protein Eng. 10:1433-1443.
    • (1997) Protein Eng. , vol.10 , pp. 1433-1443
    • Cheley, S.1    Malghani, M.S.2    Song, L.3    Hobaugh, M.4    Gouaux, J.E.5    Yang, J.6    Bayley, H.7
  • 15
    • 0020609849 scopus 로고
    • Expression of a cloned Staphylococcus aureus α-hemolysin determinant in Bacillus subtilis and Staphylococcus aureus
    • Fairweather, N., S. Kennedy, T. J. Foster, M. Kehoe, and G. Dougan. 1983. Expression of a cloned Staphylococcus aureus α-hemolysin determinant in Bacillus subtilis and Staphylococcus aureus. Infect. Immun. 41: 1112-1117.
    • (1983) Infect. Immun. , vol.41 , pp. 1112-1117
    • Fairweather, N.1    Kennedy, S.2    Foster, T.J.3    Kehoe, M.4    Dougan, G.5
  • 16
    • 0025026707 scopus 로고
    • Guide to protein purification
    • M. P. Deutcher, editor. Academic Press, New York
    • Gegenheimer, P. 1990. Guide to protein purification. In: Methods in Enzymology, Vol. 182. M. P. Deutcher, editor. Academic Press, New York, 193.
    • (1990) Methods in Enzymology , vol.182 , pp. 193
    • Gegenheimer, P.1
  • 17
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux, J. E., O. Braha, M. R. Hobaugh, L. Song, S. Cheley, C. Shustak, and H. Bayley. 1994. Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl. Acad. Sci. USA. 91:12828-12831.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 18
    • 0021747672 scopus 로고
    • Primary sequence of the α-toxin gene from Staphylococcus aureus wood 46
    • Gray, G. S., and M. Kehoe. 1984. Primary sequence of the α-toxin gene from Staphylococcus aureus Wood 46. Infect. Immun. 46:615-618.
    • (1984) Infect. Immun. , vol.46 , pp. 615-618
    • Gray, G.S.1    Kehoe, M.2
  • 20
    • 0028980231 scopus 로고
    • Protonation dynamics of the α-toxin channel from spectral analysis of pH dependent current fluctuations
    • Kasianowicz, J. J., and S. M. Bezrukov. 1995. Protonation dynamics of the α-toxin channel from spectral analysis of pH dependent current fluctuations. Biophys. J. 69:94-105.
    • (1995) Biophys. J. , vol.69 , pp. 94-105
    • Kasianowicz, J.J.1    Bezrukov, S.M.2
  • 21
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz, J. J., E. Brandin, D. Branton, and D. W. Deamer. 1996. Characterization of individual polynucleotide molecules using a membrane channel. Proc. Natl. Acad. Sci. USA. 93:13770-13773.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 24
    • 0030975688 scopus 로고    scopus 로고
    • Influence of Cys-130 S. aureus alpha-toxin on planar bilayer and erythrocyte membranes
    • Krasilnikov, O., M.-F. P. Capistrano, L. N. Yuldasheva, and R. A. Nogueira. 1997. Influence of Cys-130 S. aureus alpha-toxin on planar bilayer and erythrocyte membranes. J. Membr. Biol. 156:157-172.
    • (1997) J. Membr. Biol. , vol.156 , pp. 157-172
    • Krasilnikov, O.1    Capistrano, M.-F.P.2    Yuldasheva, L.N.3    Nogueira, R.A.4
  • 25
  • 26
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA. 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 27
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • Menestrina, G. 1986. Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations. J. Membr. Biol. 90:177-190.
    • (1986) J. Membr. Biol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 28
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and study of their properties
    • Montal, M., and P. Mueller. 1972. Formation of bimolecular membranes from lipid monolayers and study of their properties. Proc. Natl. Acad. Sci. USA. 65:3561-3566.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.65 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 29
    • 0027316337 scopus 로고
    • Staphylococcus aureus α-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cysteine at positions 69, 130, and 186
    • Palmer, M., R. Jursch, U. Weller, A. Valeva, K. Hilgert, M. Kehoe, and S. Bhakdi. 1993. Staphylococcus aureus α-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cysteine at positions 69, 130, and 186. J. Biol. Chem. 268:11959-11962.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11959-11962
    • Palmer, M.1    Jursch, R.2    Weller, U.3    Valeva, A.4    Hilgert, K.5    Kehoe, M.6    Bhakdi, S.7
  • 30
    • 0014481138 scopus 로고
    • Energy of an ion crossing a low dielectric membrane. Solution to four relevant electrostatic problems
    • Parsegian, V. A. 1969. Energy of an ion crossing a low dielectric membrane. Solution to four relevant electrostatic problems. Nature (Lond.). 221:844-846.
    • (1969) Nature (Lond.) , vol.221 , pp. 844-846
    • Parsegian, V.A.1
  • 31
    • 0023920178 scopus 로고
    • Conformational changes associated with ion permeation in L-type calcium channels
    • Pietrobon, D., B. Prod'hom, and P. Hess. 1988. Conformational changes associated with ion permeation in L-type calcium channels. Nature (Lond.). 333:373-376.
    • (1988) Nature (Lond.) , vol.333 , pp. 373-376
    • Pietrobon, D.1    Prod'hom, B.2    Hess, P.3
  • 33
    • 0029670191 scopus 로고    scopus 로고
    • Functional contributions of α5 subunit to neuronal acetylcholine receptor channels
    • Ramirez-Latorre, J., C. R. Yu, X. Qu, F. Perin, A. Karlin, and L. Role. 1996. Functional contributions of α5 subunit to neuronal acetylcholine receptor channels. Nature (Lond.). 380:347-351.
    • (1996) Nature (Lond.) , vol.380 , pp. 347-351
    • Ramirez-Latorre, J.1    Yu, C.R.2    Qu, X.3    Perin, F.4    Karlin, A.5    Role, L.6
  • 34
    • 0028077663 scopus 로고
    • Two identical noninteracting sites in an ion channel revealed by proton transfer
    • Root, M. J., and R. MacKinnon. 1994. Two identical noninteracting sites in an ion channel revealed by proton transfer. Science. 265:1852-1856.
    • (1994) Science , vol.265 , pp. 1852-1856
    • Root, M.J.1    MacKinnon, R.2
  • 35
    • 0030447720 scopus 로고    scopus 로고
    • Structure of Staphylococcal α-hemolysin, a heplameric transmembrane pore
    • Song, L., M. R. Hobaugh, C. Shustak, S. Cheley, H. Bayley, and J. E. Gouaux. 1996. Structure of Staphylococcal α-hemolysin, a heplameric transmembrane pore. Science. 274:1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 36
    • 0017667897 scopus 로고
    • Study of membrane permeability changes by fluctuation analysis
    • Stevens, C. F. 1977. Study of membrane permeability changes by fluctuation analysis. Nature (Lond). 270:391-396.
    • (1977) Nature (Lond) , vol.270 , pp. 391-396
    • Stevens, C.F.1
  • 37
    • 0024809884 scopus 로고
    • Site-directed mutagenesis of colicin-E1 provides specific attachment for spin labels whose spectra are sensitive to local conformation
    • Todd, A. P., J. Cong, F. Levinthal, C. Levinthal, and W. L. Hubbell. 1989. Site-directed mutagenesis of colicin-E1 provides specific attachment for spin labels whose spectra are sensitive to local conformation. Proteins. 6:294-305.
    • (1989) Proteins , vol.6 , pp. 294-305
    • Todd, A.P.1    Cong, J.2    Levinthal, F.3    Levinthal, C.4    Hubbell, W.L.5
  • 39
    • 0029924449 scopus 로고    scopus 로고
    • Molecular architecture of a toxin pore: A 15-residue-sequence lines the transmembrane channel of Staphylococcal alpha-toxin
    • Valeva, A., A. Weisser, B. Walker, M. Kehoe, H. Bayley, and S. Bhakdi. 1996. Molecular architecture of a toxin pore: a 15-residue-sequence lines the transmembrane channel of Staphylococcal alpha-toxin. EMBO J. 15:1857-1864.
    • (1996) EMBO J. , vol.15 , pp. 1857-1864
    • Valeva, A.1    Weisser, A.2    Walker, B.3    Kehoe, M.4    Bayley, H.5    Bhakdi, S.6
  • 40
    • 0026641089 scopus 로고
    • Functional expression of the α-hemolysin of Staphylococcus aureus in intact Escherichia coli and in cell lysates
    • Walker, B., M. Krishnasastry, L. Zorn, J. Kasianowicz, and H. Bayley. 1992. Functional expression of the α-hemolysin of Staphylococcus aureus in intact Escherichia coli and in cell lysates. J. Biol. Chem. 267:10902-10909.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10902-10909
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Kasianowicz, J.4    Bayley, H.5


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