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Volumn 90, Issue 5, 2006, Pages 1752-1766

Structural characterization and pH-induced conformational transition of full-length KcsA

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM CHANNEL; TETRAMER; BACTERIAL PROTEIN; PROKARYOTIC POTASSIUM CHANNEL;

EID: 33646145322     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.071175     Document Type: Article
Times cited : (31)

References (36)
  • 2
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 a resolution
    • Zhou, Y., J. H. Morais-Cabral, A. Kaufman, and R. MacKinnon. 2001. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature. 414:43-48.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 3
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes, D. M., L. G. Cuello, and E. Perozo. 2001. Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117:165-180.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 4
    • 0033179841 scopus 로고    scopus 로고
    • Inwardly rectifying potassium channels
    • Reimann, F., and F. M. Ashcroft. 1999. Inwardly rectifying potassium channels. Curr. Opin. Cell Biol. 11:503-508.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 503-508
    • Reimann, F.1    Ashcroft, F.M.2
  • 5
    • 0016354136 scopus 로고
    • Charge movement associated with the opening and closing of the activation gates of the Na channels
    • Armstrong, C. M., and F. Bezanilla. 1974. Charge movement associated with the opening and closing of the activation gates of the Na channels. J. Gen. Physiol. 63:533-552.
    • (1974) J. Gen. Physiol. , vol.63 , pp. 533-552
    • Armstrong, C.M.1    Bezanilla, F.2
  • 6
    • 0027971204 scopus 로고
    • Voltage gating of ion channels
    • Sigworth, F. J. 1994. Voltage gating of ion channels. Q. Rev. Biophys. 27:1-40.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 1-40
    • Sigworth, F.J.1
  • 7
    • 0035499447 scopus 로고    scopus 로고
    • Energetic optimization of ion conduction rate by the K+ selectivity filter
    • Morais-Cabral, J. H., Y. Zhou, and R. MacKinnon. 2001. Energetic optimization of ion conduction rate by the K+ selectivity filter. Nature. 414:37-42.
    • (2001) Nature , vol.414 , pp. 37-42
    • Morais-Cabral, J.H.1    Zhou, Y.2    MacKinnon, R.3
  • 8
    • 0033516590 scopus 로고    scopus 로고
    • The cavity and pore helices in the KcsA K+ channel: Electrostatic stabilization of monovalent cations
    • Roux, B., and R. MacKinnon. 1999. The cavity and pore helices in the KcsA K+ channel: electrostatic stabilization of monovalent cations. Science. 285:100-102.
    • (1999) Science , vol.285 , pp. 100-102
    • Roux, B.1    MacKinnon, R.2
  • 9
    • 0032875483 scopus 로고    scopus 로고
    • Single Streptomyces lividans K(+) channels: Functional asymmetries and sidedness of proton activation
    • Heginbotham, L., M. LeMasurier, L. Kolmakova-Partensky, and C. Miller. 1999. Single Streptomyces lividans K(+) channels: functional asymmetries and sidedness of proton activation. J. Gen. Physiol. 114: 551-560.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 551-560
    • Heginbotham, L.1    LeMasurier, M.2    Kolmakova-Partensky, L.3    Miller, C.4
  • 11
    • 0032502286 scopus 로고    scopus 로고
    • PH-dependent gating in the Streptomyces lividans K+ channel
    • Cuello, L. G., J. G. Romero, D. M. Cortes, and E. Perozo. 1998. pH-dependent gating in the Streptomyces lividans K+ channel. Biochemistry. 37:3229-3236.
    • (1998) Biochemistry , vol.37 , pp. 3229-3236
    • Cuello, L.G.1    Romero, J.G.2    Cortes, D.M.3    Perozo, E.4
  • 12
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • Liu, Y. S., P. Sompornpisut, and E. Perozo. 2001. Structure of the KcsA channel intracellular gate in the open state. Nat. Struct. Biol. 8: 883-887.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 883-887
    • Liu, Y.S.1    Sompornpisut, P.2    Perozo, E.3
  • 13
    • 0033516494 scopus 로고    scopus 로고
    • Structural rearrangements underlying K+-channel activation gating
    • Perozo, E., D. M. Cortes, and L. G. Cuello. 1999. Structural rearrangements underlying K+-channel activation gating. Science. 285: 73-78.
    • (1999) Science , vol.285 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 14
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J. Chen, M. Cadene, B. T. Chait, and R. MacKinnon. 2002. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 16
    • 85030602054 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 17
    • 0026910457 scopus 로고
    • Determination of regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. 1992. Determination of regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25:495-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 18
    • 85030608207 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 19
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. 1999. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76:2879-2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 20
    • 85030600009 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 21
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low resolution structural models
    • Kozin, M., and D. I. Svergun. 2001. Automated matching of high- and low resolution structural models. J. Appl. Crystallogr. 34:33-41.
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.1    Svergun, D.I.2
  • 23
    • 85030600552 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 24
    • 0028130511 scopus 로고
    • Detergent organization in solution and in crystals of membrane proteins
    • Timmins, P., E. Pebay-Peyroula, and W. Welte. 1994. Detergent organization in solution and in crystals of membrane proteins. Biophys. Chem. 53:27-36.
    • (1994) Biophys. Chem. , vol.53 , pp. 27-36
    • Timmins, P.1    Pebay-Peyroula, E.2    Welte, W.3
  • 25
    • 0028483318 scopus 로고
    • The maximum-entropy method without the positivity constraint: Applications to the determination of the distance-distribution function in small-angle scattering
    • Steenstrup, S., and S. Hansen. 1994. The maximum-entropy method without the positivity constraint: applications to the determination of the distance-distribution function in small-angle scattering. J. Appl. Crystallogr. 27:574-580.
    • (1994) J. Appl. Crystallogr. , vol.27 , pp. 574-580
    • Steenstrup, S.1    Hansen, S.2
  • 26
    • 0000902223 scopus 로고
    • X-ray and neutron solution scattering
    • Elsevier Science Publishers, Amsterdam
    • Perkins, S. J. 1988. X-ray and neutron solution scattering. In Modern Physical Methods in Biochemistry, Part B. Elsevier Science Publishers, Amsterdam.
    • (1988) Modern Physical Methods in Biochemistry, Part B
    • Perkins, S.J.1
  • 27
    • 0034721921 scopus 로고    scopus 로고
    • Quaternary structure of the lactose transport protein of Streptococcus thermophilus in the detergent-solubilized and membrane-reconstituted state
    • Friesen, R. H., J. Knol, and B. Poolman. 2000. Quaternary structure of the lactose transport protein of Streptococcus thermophilus in the detergent-solubilized and membrane-reconstituted state. J. Biol. Chem. 275:33527-33535.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33527-33535
    • Friesen, R.H.1    Knol, J.2    Poolman, B.3
  • 28
    • 0016640142 scopus 로고
    • Comparison of neutron and X-ray scattering of dilute myoglobin solutions
    • Ibel, K., and H. Stuhrmann. 1975. Comparison of neutron and X-ray scattering of dilute myoglobin solutions. J. Mol. Biol. 93: 255-265.
    • (1975) J. Mol. Biol. , vol.93 , pp. 255-265
    • Ibel, K.1    Stuhrmann, H.2
  • 29
  • 30
    • 0038001419 scopus 로고    scopus 로고
    • Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation
    • Heller, W. T., N. L. Finley, W. J. Dong, P. Timmins, H. C. Cheung, P. R. Rosevear, and J. Trewhella. 2003. Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation. Biochemistry. 42:7790-7800.
    • (2003) Biochemistry , vol.42 , pp. 7790-7800
    • Heller, W.T.1    Finley, N.L.2    Dong, W.J.3    Timmins, P.4    Cheung, H.C.5    Rosevear, P.R.6    Trewhella, J.7
  • 31
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. the calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S. J. 1986. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157:169-180.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 33
    • 0005548592 scopus 로고
    • X-ray scattering from a troponin C solution and its interpretation with a dumbbell shaped molecule model
    • Fujisawa, T., T. Ueki, and Y. Inoko. 1987. X-ray scattering from a troponin C solution and its interpretation with a dumbbell shaped molecule model. J. Appl. Crystallogr. 20:349-355.
    • (1987) J. Appl. Crystallogr. , vol.20 , pp. 349-355
    • Fujisawa, T.1    Ueki, T.2    Inoko, Y.3
  • 35
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • Zhou, M., J. H. Morais-Cabral, S. Mann, and R. MacKinnon. 2001. Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature. 411:657-661.
    • (2001) Nature , vol.411 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.