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Volumn 126, Issue 6, 2006, Pages 1147-1159

The RCK Domain of the KtrAB K+ Transporter: Multiple Conformations of an Octameric Ring

Author keywords

[No Author keywords available]

Indexed keywords

KTRAB ION TRANSPORTER; MEMBRANE PROTEIN; POTASSIUM CHANNEL; PROTEIN; PROTEIN KTRB; UNCLASSIFIED DRUG;

EID: 33748604768     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2006.08.028     Document Type: Article
Times cited : (78)

References (31)
  • 1
    • 0026694935 scopus 로고
    • Molecular weights of glycosylated and nonglycosylated forms of recombinant human stem cell factor determined by low-angle laser light scattering
    • Arakawa T., Langley K.E., Kameyama K., and Takagi T. Molecular weights of glycosylated and nonglycosylated forms of recombinant human stem cell factor determined by low-angle laser light scattering. Anal. Biochem. 203 (1992) 53-57
    • (1992) Anal. Biochem. , vol.203 , pp. 53-57
    • Arakawa, T.1    Langley, K.E.2    Kameyama, K.3    Takagi, T.4
  • 2
    • 0029845902 scopus 로고    scopus 로고
    • The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins
    • Bellamacina C.R. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J. 10 (1996) 1257-1269
    • (1996) FASEB J. , vol.10 , pp. 1257-1269
    • Bellamacina, C.R.1
  • 4
    • 0042862888 scopus 로고    scopus 로고
    • Functional expression of arginine kinase improves recovery from pH stress of Escherichia coli
    • Canonaco F., Schlattner U., Wallimann T., and Sauer U. Functional expression of arginine kinase improves recovery from pH stress of Escherichia coli. Biotechnol. Lett. 25 (2003) 1013-1017
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1013-1017
    • Canonaco, F.1    Schlattner, U.2    Wallimann, T.3    Sauer, U.4
  • 5
    • 8844263765 scopus 로고    scopus 로고
    • Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel
    • Clayton G.M., Silverman W.R., Heginbotham L., and Morais-Cabral J.H. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell 119 (2004) 615-627
    • (2004) Cell , vol.119 , pp. 615-627
    • Clayton, G.M.1    Silverman, W.R.2    Heginbotham, L.3    Morais-Cabral, J.H.4
  • 6
    • 29244442595 scopus 로고    scopus 로고
    • Structures of the MthK RCK domain and the effect of Ca2+ on gating ring stability
    • Dong J., Shi N., Berke I., Chen L., and Jiang Y. Structures of the MthK RCK domain and the effect of Ca2+ on gating ring stability. J. Biol. Chem. 280 (2005) 41716-41724
    • (2005) J. Biol. Chem. , vol.280 , pp. 41716-41724
    • Dong, J.1    Shi, N.2    Berke, I.3    Chen, L.4    Jiang, Y.5
  • 8
    • 0032780667 scopus 로고    scopus 로고
    • Evolutionary relationship between K(+) channels and symporters
    • Durell S.R., Hao Y., Nakamura T., Bakker E.P., and Guy H.R. Evolutionary relationship between K(+) channels and symporters. Biophys. J. 77 (1999) 775-788
    • (1999) Biophys. J. , vol.77 , pp. 775-788
    • Durell, S.R.1    Hao, Y.2    Nakamura, T.3    Bakker, E.P.4    Guy, H.R.5
  • 9
    • 1542570529 scopus 로고    scopus 로고
    • The roles and regulation of potassium in bacteria
    • Epstein W. The roles and regulation of potassium in bacteria. Prog. Nucleic Acid Res. Mol. Biol. 75 (2003) 293-320
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.75 , pp. 293-320
    • Epstein, W.1
  • 10
    • 33746486656 scopus 로고    scopus 로고
    • Oligomeric states of proteins determined by size-exclusion chromatography coupled with light scattering, absorbance and refractive index detectors
    • Nedelkov D., and Nelson R. (Eds), Humana Press, Totowa, NJ, USA
    • Folta-Stogniew E. Oligomeric states of proteins determined by size-exclusion chromatography coupled with light scattering, absorbance and refractive index detectors. In: Nedelkov D., and Nelson R. (Eds). Methods in Molecular Biology: New and Emerging Proteomics Techniques (2006), Humana Press, Totowa, NJ, USA 97-112
    • (2006) Methods in Molecular Biology: New and Emerging Proteomics Techniques , pp. 97-112
    • Folta-Stogniew, E.1
  • 11
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution:implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew E., and Williams K.M. Determination of molecular masses of proteins in solution:implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J. Biomol. Tech. 10 (1999) 51-63
    • (1999) J. Biomol. Tech. , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.M.2
  • 13
    • 0024321837 scopus 로고
    • Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography
    • Hayashi Y., Matsui H., and Takagi T. Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography. Methods Enzymol. 172 (1989) 514-528
    • (1989) Methods Enzymol. , vol.172 , pp. 514-528
    • Hayashi, Y.1    Matsui, H.2    Takagi, T.3
  • 14
    • 0033572810 scopus 로고    scopus 로고
    • Extensive regulation compromises the extent to which DNA gyrase controls DNA supercoiling and growth rate of Escherichia coli
    • Jensen P.R., Van Der Weijden C.C., Jensen L.B., Westerhoff H.V., and Snoep J.L. Extensive regulation compromises the extent to which DNA gyrase controls DNA supercoiling and growth rate of Escherichia coli. Eur. J. Biochem. 266 (1999) 865-877
    • (1999) Eur. J. Biochem. , vol.266 , pp. 865-877
    • Jensen, P.R.1    Van Der Weijden, C.C.2    Jensen, L.B.3    Westerhoff, H.V.4    Snoep, J.L.5
  • 15
    • 0035054180 scopus 로고    scopus 로고
    • Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel
    • Jiang Y., Pico A., Cadene M., Chait B.T., and MacKinnon R. Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel. Neuron 29 (2001) 593-601
    • (2001) Neuron , vol.29 , pp. 593-601
    • Jiang, Y.1    Pico, A.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 16
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., and MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417 (2002) 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
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 22
    • 11144226383 scopus 로고    scopus 로고
    • Na+-dependent K+ uptake Ktr system from the cyanobacterium Synechocystis sp. PCC 6803 and its role in the early phases of cell adaptation to hyperosmotic shock
    • Matsuda N., Kobayashi H., Katoh H., Ogawa T., Futatsugi L., Nakamura T., Bakker E.P., and Uozumi N. Na+-dependent K+ uptake Ktr system from the cyanobacterium Synechocystis sp. PCC 6803 and its role in the early phases of cell adaptation to hyperosmotic shock. J. Biol. Chem. 279 (2004) 54952-54962
    • (2004) J. Biol. Chem. , vol.279 , pp. 54952-54962
    • Matsuda, N.1    Kobayashi, H.2    Katoh, H.3    Ogawa, T.4    Futatsugi, L.5    Nakamura, T.6    Bakker, E.P.7    Uozumi, N.8
  • 23
    • 0026036336 scopus 로고
    • The cloning and DNA sequence of the gene for the glutathione-regulated potassium-efflux system KefC of Escherichia coli
    • Munro A.W., Ritchie G.Y., Lamb A.J., Douglas R.M., and Booth I.R. The cloning and DNA sequence of the gene for the glutathione-regulated potassium-efflux system KefC of Escherichia coli. Mol. Microbiol. 5 (1991) 607-616
    • (1991) Mol. Microbiol. , vol.5 , pp. 607-616
    • Munro, A.W.1    Ritchie, G.Y.2    Lamb, A.J.3    Douglas, R.M.4    Booth, I.R.5
  • 24
    • 0031800822 scopus 로고    scopus 로고
    • KtrAB, a new type of bacterial K(+)-uptake system from Vibrio alginolyticus
    • Nakamura T., Yuda R., Unemoto T., and Bakker E.P. KtrAB, a new type of bacterial K(+)-uptake system from Vibrio alginolyticus. J. Bacteriol. 180 (1998) 3491-3494
    • (1998) J. Bacteriol. , vol.180 , pp. 3491-3494
    • Nakamura, T.1    Yuda, R.2    Unemoto, T.3    Bakker, E.P.4
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0037077136 scopus 로고    scopus 로고
    • A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch
    • Roosild T.P., Miller S., Booth I.R., and Choe S. A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch. Cell 109 (2002) 781-791
    • (2002) Cell , vol.109 , pp. 781-791
    • Roosild, T.P.1    Miller, S.2    Booth, I.R.3    Choe, S.4
  • 27
    • 0027239791 scopus 로고
    • NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence similarity between TrkA and domains of a family of dehydrogenases suggest a role for NAD+ in bacterial transport
    • Schlosser A., Hamann A., Bossemeyer D., Schneider E., and Bakker E.P. NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence similarity between TrkA and domains of a family of dehydrogenases suggest a role for NAD+ in bacterial transport. Mol. Microbiol. 9 (1993) 533-543
    • (1993) Mol. Microbiol. , vol.9 , pp. 533-543
    • Schlosser, A.1    Hamann, A.2    Bossemeyer, D.3    Schneider, E.4    Bakker, E.P.5
  • 28
    • 0032921035 scopus 로고    scopus 로고
    • Change to alanine of one out of four selectivity filter glycines in KtrB causes a two orders of magnitude decrease in the affinities for both K+ and Na+ of the Na+ dependent K+ uptake system KtrAB from Vibrio alginolyticus
    • Tholema N., Bakker E.P., Suzuki A., and Nakamura T. Change to alanine of one out of four selectivity filter glycines in KtrB causes a two orders of magnitude decrease in the affinities for both K+ and Na+ of the Na+ dependent K+ uptake system KtrAB from Vibrio alginolyticus. FEBS Lett. 450 (1999) 217-220
    • (1999) FEBS Lett. , vol.450 , pp. 217-220
    • Tholema, N.1    Bakker, E.P.2    Suzuki, A.3    Nakamura, T.4
  • 29
    • 29244468878 scopus 로고    scopus 로고
    • All four putative selectivity filter glycine residues in KtrB are essential for high affinity and selective K+ uptake by the KtrAB system from Vibrio alginolyticus
    • Tholema N., Vor der Bruggen M., Maser P., Nakamura T., Schroeder J.I., Kobayashi H., Uozumi N., and Bakker E.P. All four putative selectivity filter glycine residues in KtrB are essential for high affinity and selective K+ uptake by the KtrAB system from Vibrio alginolyticus. J. Biol. Chem. 280 (2005) 41146-41154
    • (2005) J. Biol. Chem. , vol.280 , pp. 41146-41154
    • Tholema, N.1    Vor der Bruggen, M.2    Maser, P.3    Nakamura, T.4    Schroeder, J.I.5    Kobayashi, H.6    Uozumi, N.7    Bakker, E.P.8
  • 30
    • 33748622291 scopus 로고    scopus 로고
    • Crystal structures of a ligand-free MthK gating ring: insights into the ligand gating mechanism of K+ channels
    • this issue
    • Ye S., Li Y., Chen L., and Jiang Y. Crystal structures of a ligand-free MthK gating ring: insights into the ligand gating mechanism of K+ channels. Cell 126 (2006) 1161-1173 this issue
    • (2006) Cell , vol.126 , pp. 1161-1173
    • Ye, S.1    Li, Y.2    Chen, L.3    Jiang, Y.4
  • 31
    • 0242424106 scopus 로고    scopus 로고
    • Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus
    • Yernool D., Boudker O., Folta-Stogniew E., and Gouaux E. Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus. Biochemistry 42 (2003) 12981-12988
    • (2003) Biochemistry , vol.42 , pp. 12981-12988
    • Yernool, D.1    Boudker, O.2    Folta-Stogniew, E.3    Gouaux, E.4


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