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Volumn 203, Issue 1, 2000, Pages 29-33

Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase

Author keywords

ATP synthase; Cross linking; Electron microscopy; F1F(o) type ATPase; Rotation

Indexed keywords

CROSS LINKING REAGENT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0033971704     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (63)

References (43)
  • 3
    • 0026788447 scopus 로고
    • 1) via cysteines introduced by site-directed mutagenesis
    • 1) via cysteines introduced by site-directed mutagenesis. J. Biol. Chem. 267, 21355-21359.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21355-21359
    • Aggeler, R.1    Capaldi, R.A.2
  • 5
    • 0026577596 scopus 로고
    • 1 ATPase. Modification of these sites with tetrafluorophenlyazide-maleimides and examination of changes in the binding of the ε subunit when different nucleotides are in catalytic sites
    • 1 ATPase. Modification of these sites with tetrafluorophenlyazide-maleimides and examination of changes in the binding of the ε subunit when different nucleotides are in catalytic sites. Biochemistry 31, 2956-2961.
    • (1992) Biochemistry , vol.31 , pp. 2956-2961
    • Aggeler, R.1    Chicas-Cruz, K.2    Cai, S.-X.3    Keana, J.F.W.4    Capaldi, R.A.5
  • 8
    • 0031445914 scopus 로고    scopus 로고
    • Visualization of the peripheral stalk in V-type ATPase: Evidence for a stator structure essential to rotational catalysis
    • Boekema, E. J., Ubbink-Kok, T., Lolkema, J. S., Brisson, A. and Konings, W. N. (1997). Visualization of the peripheral stalk in V-type ATPase: evidence for a stator structure essential to rotational catalysis. Proc. Natl. Acad. Sci. USA 94, 14291-14293.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14291-14293
    • Boekema, E.J.1    Ubbink-Kok, T.2    Lolkema, J.S.3    Brisson, A.4    Konings, W.N.5
  • 10
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - Some probabilities and possibilities
    • Boyer, P. D. (1993). The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215-250.
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 12
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • Cherepanov, D. A., Mulkidjanian, A. Y. and Junge, W. (1999). Transient accumulation of elastic energy in proton translocating ATP synthase. FEBS Lett. 449, 1-6.
    • (1999) FEBS Lett. , vol.449 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 13
    • 0021766172 scopus 로고
    • The mechanism of ATP synthase: Conformational changes by rotation of the b subunit
    • Cox, G. B., Jans, D. A., Fimmel, A. L., Gibson, F. and Hatch, L. (1984). The mechanism of ATP synthase: conformational changes by rotation of the b subunit. Biochim. Biophys. Acta 768, 201-208.
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 201-208
    • Cox, G.B.1    Jans, D.A.2    Fimmel, A.L.3    Gibson, F.4    Hatch, L.5
  • 16
    • 0000936565 scopus 로고
    • Cell membrane ultrastructure. Low temperature electron microscopy and X-ray diffraction of lipoprotein components in lamellar systems
    • Fernandez-Moran, H. (1962). Cell membrane ultrastructure. Low temperature electron microscopy and X-ray diffraction of lipoprotein components in lamellar systems. Circulation 26, 1039-1065.
    • (1962) Circulation , vol.26 , pp. 1039-1065
    • Fernandez-Moran, H.1
  • 17
    • 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
  • 19
    • 0023666442 scopus 로고
    • 0 domains of ATP synthase visualized by electron microscopy of unstained specimens
    • 0 domains of ATP synthase visualized by electron microscopy of unstained specimens. FEBS Lett. 219, 274-278.
    • (1987) FEBS Lett. , vol.219 , pp. 274-278
    • Gogol, E.P.1    Lücken, U.2    Capaldi, R.A.3
  • 21
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotary mechanics
    • Junge, W., Lill, H. and Engelbrecht, S. (1997). ATP synthase: an electrochemical transducer with rotary mechanics. Trends Biochem. Sci. 22, 420-423.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 27
  • 29
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • Sabbert, D., Engelbrecht, S. and Junge, W. (1996). Intersubunit rotation in active F-ATPase. Nature 381, 623-625.
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 31
    • 0018787614 scopus 로고
    • Mitochondrial ATPase complex. A dispersed, cytochrome deficient, oligomycin-sensitive preparation from rat liver mitochondria containing molecules with a tripartite structural arrangement
    • Soper, J. W., Decker, G. L. and Pederson, P. L. (1979). Mitochondrial ATPase complex. A dispersed, cytochrome deficient, oligomycin-sensitive preparation from rat liver mitochondria containing molecules with a tripartite structural arrangement. J. Biol Chem. 254, 11170-11176.
    • (1979) J. Biol Chem. , vol.254 , pp. 11170-11176
    • Soper, J.W.1    Decker, G.L.2    Pederson, P.L.3
  • 34
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the ε subunit of the proton translocating ATP synthase from E. coli
    • Uhlin, U., Cox, G. B. and Goss, J. M. (1997). Crystal structure of the ε subunit of the proton translocating ATP synthase from E. coli. Structure 5, 1219-1230.
    • (1997) Structure , vol.5 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Goss, J.M.3
  • 35
    • 0029854749 scopus 로고    scopus 로고
    • 0 parts and can interact with both the ε and the c oligomer
    • 0 parts and can interact with both the ε and the c oligomer. J. Biol. Chem. 271, 28341-28347.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28341-28347
    • Watts, S.D.1    Tang, C.2    Capaldi, R.A.3
  • 37
    • 2642707545 scopus 로고    scopus 로고
    • 0 part in the E. coli ATP synthase. A rotor and a stator?
    • 0 part in the E. coli ATP synthase. A rotor and a stator? Nature 393, 29.
    • (1998) Nature , vol.393 , pp. 29
    • Wilkens, S.1    Capaldi, R.A.2
  • 39
    • 0032500380 scopus 로고    scopus 로고
    • 1 ATPase from E. coli and interactions of this subunit with β subunits in the complex
    • 1 ATPase from E. coli and interactions of this subunit with β subunits in the complex. J. Biol. Chem. 273, 26645-26651.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26645-26651
    • Wilkens, S.1    Capaldi, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.