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Volumn 203, Issue 1, 2000, Pages 1-8

Rotation of F1-ATPase and the hinge residues of the β subunit

Author keywords

F1 ATPase; F1F0 ATP synthase; Motor protein; Rotation; Single molecule observation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBUNIT; FLUORESCENCE; HYDROLYSIS; IMMOBILIZED ENZYME;

EID: 0033975117     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (53)

References (22)
  • 3
    • 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
  • 4
    • 0002888351 scopus 로고
    • The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts
    • (ed. B. Selman and S. Selman-Reiner), New York: North Holland Elsevier
    • Boyer, P. D. and Kohlbrenner, W. E. (1981). The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts. In Energy Coupling in Photosynthesis (ed. B. Selman and S. Selman-Reiner), pp. 231-240. New York: North Holland Elsevier.
    • (1981) Energy Coupling in Photosynthesis , pp. 231-240
    • Boyer, P.D.1    Kohlbrenner, W.E.2
  • 7
    • 0011364439 scopus 로고
    • Structural studies of myosin:Nucleotide complexes: A revised model for the molecular basis of muscle contraction
    • Fisher, A. J., Smith, C. A., Thoden, J., Smith, R., Sutoh, K., Holden, H. M. and Rayment, I. (1995b). Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction. Biophys. J. 68, 19-28.
    • (1995) Biophys. J. , vol.68 , pp. 19-28
    • Fisher, A.J.1    Smith, C.A.2    Thoden, J.3    Smith, R.4    Sutoh, K.5    Holden, H.M.6    Rayment, I.7
  • 9
    • 0029417124 scopus 로고
    • 1-ATPase from the thermophilic Bacillus PS3 containing the α-D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites
    • 1-ATPase from the thermophilic Bacillus PS3 containing the α-D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites. Biochemistry 34, 16412-16418.
    • (1995) Biochemistry , vol.34 , pp. 16412-16418
    • Jault, J.M.1    Matsui, T.2    Jault, F.M.3    Kaibara, C.4    Muneyuki, E.5    Yoshida, M.6    Kagawa, Y.7    Allison, W.S.8
  • 12
    • 0026610270 scopus 로고
    • sα highlights the requirement for dissociation of G protein subunits
    • sα highlights the requirement for dissociation of G protein subunits. J. Biol. Chem. 267, 1212-1218.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1212-1218
    • Lee, E.1    Taussig, R.2    Gilman, A.G.3
  • 14
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-α complexed with GTPγS
    • Noel, J. P., Hamm, H. E. and Sigler, P. B. (1993). The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366, 654-662.
    • (1993) Nature , vol.366 , pp. 654-662
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 17
    • 0032493769 scopus 로고    scopus 로고
    • Mutational analysis of the switch II loop of Dictyostelium myosin II
    • Sasaki, N., Shimada, T. and Sutoh, K. (1998). Mutational analysis of the switch II loop of Dictyostelium myosin II. J. Biol. Chem. 273, 20334-20340.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20334-20340
    • Sasaki, N.1    Shimada, T.2    Sutoh, K.3
  • 18
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II)·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith, C. A. and Rayment, I. (1996). X-ray structure of the magnesium(II)·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry 35, 5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 19
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda, K., Schmidt, C. F., Schnapp, B. J. and Block, S. M. (1993). Direct observation of kinesin stepping by optical trapping interferometry. Nature 365, 721-727.
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 22
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps. Cell 93, 1117-1124.
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinoshita, K.3    Yoshida, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.