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Volumn 75, Issue 5, 1998, Pages 2212-2219

A model of the quaternary structure of the Escherichia coli F1 ATPase from X-ray solution scattering and evidence for structural changes in the Delta subunit during ATP hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 0031751233     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77665-9     Document Type: Article
Times cited : (28)

References (51)
  • 4
    • 0017182260 scopus 로고
    • An automated continuous assay of membrane-bound and soluble ATPases and related enzymes
    • Arnold, A., H. U. Wolf, B. P. Ackermann, and H. Bader. 1976. An automated continuous assay of membrane-bound and soluble ATPases and related enzymes. Anal. Biochem. 71:209-213.
    • (1976) Anal. Biochem. , vol.71 , pp. 209-213
    • Arnold, A.1    Wolf, H.U.2    Ackermann, B.P.3    Bader, H.4
  • 9
    • 0024033744 scopus 로고
    • Data acquisition systems for linear and area X-ray detectors using delay line readout
    • Boulin, C. J., R. Kempf, A. Gabriel, and M. H. J. Koch. 1988. Data acquisition systems for linear and area X-ray detectors using delay line readout. Nucl. Instrum. Methods. A269:312-320.
    • (1988) Nucl. Instrum. Methods , vol.A269 , pp. 312-320
    • Boulin, C.J.1    Kempf, R.2    Gabriel, A.3    Koch, M.H.J.4
  • 10
    • 0022787110 scopus 로고
    • Data appraisal, evaluation and display for synchroton radiation experiments: Hardware and software
    • Boulin, C., R. Kempf, M. H. J. Koch, and S. M. McLaughlin. 1986. Data appraisal, evaluation and display for synchroton radiation experiments: hardware and software. Nucl. Instrum. Methods. A249:399-407.
    • (1986) Nucl. Instrum. Methods , vol.A249 , pp. 399-407
    • Boulin, C.1    Kempf, R.2    Koch, M.H.J.3    McLaughlin, S.M.4
  • 11
    • 0023044945 scopus 로고
    • 1 adenosine triphosphate of Escherichia coli
    • 1 adenosine triphosphate of Escherichia coli. Biochim. Biophys. Acta. 851:385-394.
    • (1986) Biochim. Biophys. Acta. , vol.851 , pp. 385-394
    • Bragg, P.D.1    Hou, C.2
  • 14
    • 0016642871 scopus 로고
    • A simple technique for eliminating interference by detergents in the Lowry method of protein determination
    • Dulley, J. R., and P. Gieve. 1975. A simple technique for eliminating interference by detergents in the Lowry method of protein determination. Anal. Biochem. 64:136-147.
    • (1975) Anal. Biochem. , vol.64 , pp. 136-147
    • Dulley, J.R.1    Gieve, P.2
  • 15
    • 0030863908 scopus 로고    scopus 로고
    • ATP synthase, a tentative structural model
    • Engelbrecht, S., and W. Junge. 1997. ATP synthase, a tentative structural model. FEBS Lett. 414:484-491.
    • (1997) FEBS Lett. , vol.414 , pp. 484-491
    • Engelbrecht, S.1    Junge, W.2
  • 18
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C. H., and Y. Subbarow. 1925. The colorimetric determination of phosphorus. J. Biol. Chem. 66:375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 19
    • 0019067193 scopus 로고
    • The localization method used at EMBL
    • Gabriel, A., and F. Dauvergne. 1982. The localization method used at EMBL. Nucl. Instrum. Methods. 201:223-224.
    • (1982) Nucl. Instrum. Methods , vol.201 , pp. 223-224
    • Gabriel, A.1    Dauvergne, F.2
  • 20
    • 0024372288 scopus 로고
    • 1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex
    • 1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex. Biochemistry. 28:4717-4724.
    • (1989) Biochemistry , vol.28 , pp. 4717-4724
    • Gogol, E.P.1    Aggeler, R.2    Sagermann, M.3    Capaldi, R.A.4
  • 22
    • 5344261738 scopus 로고    scopus 로고
    • 3H] 2-azido-ATP using the mutant βGlu381Cys:∈Ser108Cys to identify different β subunits by their interactions
    • 3H] 2-azido-ATP using the mutant βGlu381Cys:∈Ser108Cys to identify different β subunits by their interactions. Biochemistry. 35:3875-3879.
    • (1996) Biochemistry , vol.35 , pp. 3875-3879
    • Grüber, G.1    Capaldi, R.A.2
  • 23
    • 0030450752 scopus 로고    scopus 로고
    • 1 ATPase by disulfide bond formation: Effect on nucleotide binding affinities on the catalytic sites
    • 1 ATPase by disulfide bond formation: effect on nucleotide binding affinities on the catalytic sites. J. Biol. Chem. 271:32623-32628.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32623-32628
    • Grüber, G.1    Capaldi, R.A.2
  • 24
    • 0030611891 scopus 로고    scopus 로고
    • o by using a cytochrome bo-deficient strain of Escherichia coli facilitates crystallization of these complexes
    • o by using a cytochrome bo-deficient strain of Escherichia coli facilitates crystallization of these complexes. FEBS Lett. 410:165-168.
    • (1997) FEBS Lett. , vol.410 , pp. 165-168
    • Grüber, G.1    Hausrath, A.2    Sagermann, M.3    Capaldi, R.A.4
  • 25
    • 0020114103 scopus 로고
    • X-ray diffraction and scattering on disordered systems using synchroton radiation
    • Koch, M. H. J., and J. Bordas. 1983. X-ray diffraction and scattering on disordered systems using synchroton radiation. Nucl. Instrum. Methods. 208:461-469.
    • (1983) Nucl. Instrum. Methods , vol.208 , pp. 461-469
    • Koch, M.H.J.1    Bordas, J.2
  • 26
    • 33751135474 scopus 로고    scopus 로고
    • ASSA - A program for three dimensional rendering in solution scattering from biopolymers
    • Kozin, M. B., V. V. Volkov, and D. I. Svergun. 1997. ASSA - a program for three dimensional rendering in solution scattering from biopolymers. J. Appl. Crystallogr. 30:811-815.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 811-815
    • Kozin, M.B.1    Volkov, V.V.2    Svergun, D.I.3
  • 28
    • 0025871645 scopus 로고
    • Structure-function relationships of domains of the δ subunit in Escherichia coli adenosine triphosphatase
    • Mendel-Hartvig, J., and R. A. Capaldi. 1991. Structure-function relationships of domains of the δ subunit in Escherichia coli adenosine triphosphatase. Biochim. Biophys. Acta. 1060:115-124.
    • (1991) Biochim. Biophys. Acta. , vol.1060 , pp. 115-124
    • Mendel-Hartvig, J.1    Capaldi, R.A.2
  • 30
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 32
    • 65449121560 scopus 로고
    • Ein neues Verfahren zur Bestimmung der Oberflächenform und der inneren Struktur von gelösten globulären Proteinen aus Röntgenkleinwinkelmessungen
    • Stuhrmann, H. B. 1970. Ein neues Verfahren zur Bestimmung der Oberflächenform und der inneren Struktur von gelösten globulären Proteinen aus Röntgenkleinwinkelmessungen. Zeitschr. Physik. Chem. Neue Folge. 72:177-198.
    • (1970) Zeitschr. Physik. Chem. Neue Folge , vol.72 , pp. 177-198
    • Stuhrmann, H.B.1
  • 33
    • 0026910457 scopus 로고
    • Determination of the regularization parameters in indirect transform methods using perceptual criteria
    • Svergun, D. I. 1992. Determination of the regularization parameters 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
  • 34
    • 0027578071 scopus 로고
    • A direct method of small-angle scattering data treatment
    • Svergun, D. I. 1993. A direct method of small-angle scattering data treatment. J. Appl. Crystallogr. 26:258-267.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 258-267
    • Svergun, D.I.1
  • 35
    • 0001540719 scopus 로고
    • Solution scattering from biopolymers: Advanced contrast variation data analysis
    • Svergun, D. I. 1994. Solution scattering from biopolymers: advanced contrast variation data analysis. Acta Crystallogr. A50:391-402.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 391-402
    • Svergun, D.I.1
  • 36
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D. I., C. Barberato, and M. H. J. Koch. 1995. CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28:768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 37
    • 0031027047 scopus 로고    scopus 로고
    • Large differences are observed between the crystal and solution quaternary structures of allosteric aspartate transcarbamylase in the R state
    • Svergun, D. I., C. Barberato, M. H. J. Koch, L. Fetler, and P. Vachette. 1997a. Large differences are observed between the crystal and solution quaternary structures of allosteric aspartate transcarbamylase in the R state. Proteins. 27:110-117.
    • (1997) Proteins , vol.27 , pp. 110-117
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3    Fetler, L.4    Vachette, P.5
  • 39
    • 84944815124 scopus 로고
    • Small-angle scattering data treatment by the regularization method
    • Svergun, D. I., A. V. Semenyuk, and L. A. Feigin. 1988. Small-angle scattering data treatment by the regularization method. Acta Crystallogr. A44:244-250.
    • (1988) Acta Crystallogr. , vol.A44 , pp. 244-250
    • Svergun, D.I.1    Semenyuk, A.V.2    Feigin, L.A.3
  • 40
    • 84945101258 scopus 로고
    • New developments in direct shape determination from small-angle scattering. 1. Theory and model calculations
    • Svergun, D. I., and H. B. Stuhrmann. 1991. New developments in direct shape determination from small-angle scattering. 1. Theory and model calculations. Acta Crystallogr. A47:736-744.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 736-744
    • Svergun, D.I.1    Stuhrmann, H.B.2
  • 41
    • 0001252801 scopus 로고    scopus 로고
    • New developments in direct shape determination from small-angle scattering. 2. Uniqueness
    • Svergun, D. I., V. V. Volkov, M. B. Kozin, and H. B. Stuhrmann. 1996. New developments in direct shape determination from small-angle scattering. 2. Uniqueness. Acta Crystallogr. A52:419-426.
    • (1996) Acta Crystallogr. , vol.A52 , pp. 419-426
    • Svergun, D.I.1    Volkov, V.V.2    Kozin, M.B.3    Stuhrmann, H.B.4
  • 44
    • 0344600354 scopus 로고
    • ATP Hydrolysis-driven structural changes in the γ subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues
    • Turina, P., and R. A. Capaldi. 1994. ATP Hydrolysis-driven structural changes in the γ subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues. J. Biol. Chem. 272:19621-19624.
    • (1994) J. Biol. Chem. , vol.272 , pp. 19621-19624
    • Turina, P.1    Capaldi, R.A.2
  • 45
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the ∈ subunit of the proton-translocating ATP synthase from Escherichia coli
    • Uhlin, U., G. B. Cox, and J. M. Guss. 1997. Crystal structure of the ∈ subunit of the proton-translocating ATP synthase from Escherichia coli. Structure. 5:1219-1230.
    • (1997) Structure , vol.5 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Guss, J.M.3
  • 46
    • 0030592112 scopus 로고    scopus 로고
    • o-ATP synthase: Development of direct optical probes of the catalytic mechanism
    • o-ATP synthase: development of direct optical probes of the catalytic mechanism. Biochim. Biophys. Acta. 1275:101-104.
    • (1996) Biochim. Biophys. Acta. , vol.1275 , pp. 101-104
    • Weber, J.1    Senior, A.E.2
  • 48
    • 0028970620 scopus 로고
    • Structural features of the ∈ subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
    • Wilkens, S., F. W. Dahlquist, L. P. McIntosh, L. W. Donaldson, and R. A. Capaldi. 1995. Structural features of the ∈ subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nature Struct. Biol. 2:961-967.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 961-967
    • Wilkens, S.1    Dahlquist, F.W.2    McIntosh, L.P.3    Donaldson, L.W.4    Capaldi, R.A.5
  • 49
    • 0031055743 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the δ subunit of the E. coli ATP synthase
    • Wilkens, S., S. D. Dunn, J. Chandler, F. W. Dahlquist, and R. A. Capaldi. 1996. Solution structure of the N-terminal domain of the δ subunit of the E. coli ATP synthase. Nature Struct. Biol. 4:198-201.
    • (1996) Nature Struct. Biol. , vol.4 , pp. 198-201
    • Wilkens, S.1    Dunn, S.D.2    Chandler, J.3    Dahlquist, F.W.4    Capaldi, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.