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Volumn 203, Issue 1, 2000, Pages 9-17

Coupling H+ transport to rotary catalysis in F-type ATP synthases: Structure and organization of the transmembrane rotary motor

Author keywords

ATP synthase; Cross linking; Escherichia coli; F0 structure; Molecular modelling; Nuclear magnetic resonance; Proton transport; Rotary motor; Subunit c

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0033960457     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (117)

References (51)
  • 5
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer, P. D. (1997). The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66, 717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 6
    • 0033529291 scopus 로고    scopus 로고
    • 0, ATP synthase: Model derived from solution structure of the monomer and cross-linking in the native enzyme
    • 0, ATP synthase: Model derived from solution structure of the monomer and cross-linking in the native enzyme. Proc. Natl. Acad. Sci. USA 96, 7785-7790.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7785-7790
    • Dmitriev, O.Y.1    Jones, P.C.2    Fillingame, R.H.3
  • 9
    • 0032502352 scopus 로고    scopus 로고
    • 2δ complex from Escherichia coli ATP synthase
    • 2δ complex from Escherichia coli ATP synthase. J. Biol. Chem. 273, 8646-8651.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8646-8651
    • Dunn, S.D.1    Chandler, J.2
  • 10
    • 0032576724 scopus 로고    scopus 로고
    • Energy transduction in ATP synthase
    • Elston, T., Wang, H. and Oster, G. (1998). Energy transduction in ATP synthase. Nature 391, 510-513.
    • (1998) Nature , vol.391 , pp. 510-513
    • Elston, T.1    Wang, H.2    Oster, G.3
  • 11
    • 0030863908 scopus 로고    scopus 로고
    • ATP synthase: A tentative structural model
    • Engelbrecht, S. and Junge, W. (1997). ATP synthase: a tentative structural model. FEBS Lett. 414, 485-491.
    • (1997) FEBS Lett. , vol.414 , pp. 485-491
    • Engelbrecht, S.1    Junge, W.2
  • 12
    • 0030898875 scopus 로고    scopus 로고
    • 0 ATP synthases: Glimpses of interacting parts in a dynamic molecular machine
    • 0 ATP synthases: glimpses of interacting parts in a dynamic molecular machine. J. Exp. Biol. 200, 217-224.
    • (1997) J. Exp. Biol. , vol.200 , pp. 217-224
    • Fillingame, R.H.1
  • 14
    • 0025719966 scopus 로고
    • 0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide
    • 0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide. J. Biol. Chem. 266, 20934-20939.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20934-20939
    • Fillingame, R.H.1    Oldenburg, M.2    Fraga, D.3
  • 17
    • 0028070757 scopus 로고
    • 0 suggested by suppressor mutations to Asp24Gly61 mutant of ATP synthase subunit c
    • 0 suggested by suppressor mutations to Asp24Gly61 mutant of ATP synthase subunit c. J. Biol. Chem. 269, 2562-2567.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2562-2567
    • Fraga, D.1    Hermolin, J.2    Fillingame, R.H.3
  • 19
    • 0032493845 scopus 로고    scopus 로고
    • Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesis
    • Groth, G., Tilg, Y. and Schirwitz, K. (1998). Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesis J. Mol. Biol. 281, 49-59.
    • (1998) J. Mol. Biol. , vol.281 , pp. 49-59
    • Groth, G.1    Tilg, Y.2    Schirwitz, K.3
  • 20
    • 0030845490 scopus 로고    scopus 로고
    • Model of the c-subunit oligomer in the membrane domain of F-ATPases
    • Groth, G. and Walker, J. E. (1997). Model of the c-subunit oligomer in the membrane domain of F-ATPases. FEBS Lett. 410, 117-123.
    • (1997) FEBS Lett. , vol.410 , pp. 117-123
    • Groth, G.1    Walker, J.E.2
  • 22
    • 0032499690 scopus 로고    scopus 로고
    • 0 ATP synthase of Escherichia coli defined by disulfide cross-linking
    • 0 ATP synthase of Escherichia coli defined by disulfide cross-linking. Proc. Natl. Acad. Sci. USA 95, 6607-661.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6607-6661
    • Jiang, W.1    Fillingame, R.H.2
  • 23
    • 0032491417 scopus 로고    scopus 로고
    • +-transporting ATP synthase: Functional dimers and trimers and determination of stoichiometry by cross-linking analysis
    • +-transporting ATP synthase: Functional dimers and trimers and determination of stoichiometry by cross-linking analysis. J. Biol. Chem. 273, 29701-29705.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29701-29705
    • Jones, P.C.1    Fillingame, R.H.2
  • 25
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge, W., Lill, H. and Engelbrecht, S. (1997). ATP synthase: An electrochemical transducer with rotatory 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
  • 26
    • 0030809240 scopus 로고    scopus 로고
    • + in the c subunit of the ATP synthase from Propionigenium modestum
    • + in the c subunit of the ATP synthase from Propionigenium modestum. Biochemistry 36, 9185-9194.
    • (1997) Biochemistry , vol.36 , pp. 9185-9194
    • Kaim, G.1    Wehrle, F.2    Gerike, U.3    Dimroth, P.4
  • 27
    • 0032568845 scopus 로고    scopus 로고
    • 0 ATP synthase as determined by labeling of unique cysteine residues
    • 0 ATP synthase as determined by labeling of unique cysteine residues. J. Biol. Chem. 273, 16235-16240.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16235-16240
    • Long, J.C.1    Wang, S.2    Vik, S.B.3
  • 28
    • 0021772468 scopus 로고
    • +-translocating adenosinetriphosphate complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-[3-(dimethylamino)propyl]-carbodiimide and effect on the proton channeling function
    • +-translocating adenosinetriphosphate complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-[3-(dimethylamino)propyl]-carbodiimide and effect on the proton channeling function. Biochemistry 23, 4128-4134.
    • (1984) Biochemistry , vol.23 , pp. 4128-4134
    • Lötscher, H.-R.1    DeJong, C.2    Capaldi, R.A.3
  • 30
    • 0026787745 scopus 로고
    • Structural conservation and functional diversity of V-ATPases
    • Nelson, N. (1992). Structural conservation and functional diversity of V-ATPases. J. Bioenerg. Biomembr. 24, 407-414.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 407-414
    • Nelson, N.1
  • 32
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi, V K. and Girvin, M. E. (1999). Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402, 263-268.
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi K. V1    Girvin, M.E.2
  • 33
    • 0032491567 scopus 로고    scopus 로고
    • 1 via an α-subunit in the Escherichia coli ATP synthase
    • 1 via an α-subunit in the Escherichia coli ATP synthase. J. Biol. Chem. 273, 29406-29410.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29406-29410
    • Rodgers, A.J.W.1    Capaldi, R.A.2
  • 34
    • 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
  • 38
    • 0027970177 scopus 로고
    • 0 ATP synthases suggested by double mutants of the a subunit
    • 0 ATP synthases suggested by double mutants of the a subunit. J. Biol. Chem. 269, 30364-30369.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 39
    • 0032568844 scopus 로고    scopus 로고
    • 0 ATP synthase near His245 and implications on gating of the proton channel
    • 0 ATP synthase near His245 and implications on gating of the proton channel. J. Biol. Chem. 273, 16229-16234.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16229-16234
    • Vik, S.B.1    Patterson, A.R.2    Antonio, B.J.3
  • 40
    • 0020439660 scopus 로고
    • The membrane bound ATP synthase of Escherichia coli: A review of structural and functional analyses of the atp operon
    • von Meyenburg, K., Jorgensen, B. B., Nielsen, J., Hansen, F. G. and Michelsen, O. (1982). The membrane bound ATP synthase of Escherichia coli: A review of structural and functional analyses of the atp operon. Tokai J. Exp. Clin. Med. 7 (Suppl.), 23-31.
    • (1982) Tokai J. Exp. Clin. Med. , vol.7 , Issue.SUPPL. , pp. 23-31
    • Von Meyenburg, K.1    Jorgensen, B.B.2    Nielsen, J.3    Hansen, F.G.4    Michelsen, O.5
  • 41
    • 0033546193 scopus 로고    scopus 로고
    • A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase
    • Wada, T., Long, J. C., Zhang, D. and Vik, S. B. (1999) A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase. J. Biol. Chem. 274, 17353-17357.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17353-17357
    • Wada, T.1    Long, J.C.2    Zhang, D.3    Vik, S.B.4
  • 42
    • 0032544312 scopus 로고    scopus 로고
    • ATP synthesis by rotary catalysis (Nobel lecture)
    • Walker, J. E. (1998). ATP synthesis by rotary catalysis (Nobel lecture). Angew. Chem. Int. Ed 37, 2308-2319.
    • (1998) Angew. Chem. Int. Ed , vol.37 , pp. 2308-2319
    • Walker, J.E.1
  • 43
    • 0029854749 scopus 로고    scopus 로고
    • 0 interface in the binding site for the c subunit ring
    • 0 interface in the binding site for the c subunit ring. 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
  • 45
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • Wiener, M. C. and White, S. H. (1992). Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys. J. 61, 434-447.
    • (1992) Biophys. J. , vol.61 , pp. 434-447
    • Wiener, M.C.1    White, S.H.2
  • 46
    • 2642707545 scopus 로고    scopus 로고
    • ATP synthase's second stalk comes into focus
    • Wilkens, S. and Capaldi, R. A. (1998). ATP synthase's second stalk comes into focus. Nature 393, 29.
    • (1998) Nature , vol.393 , pp. 29
    • Wilkens, S.1    Capaldi, R.A.2
  • 47
    • 0028970620 scopus 로고
    • Structural features of the ε subunit of the Escherichia coli ATP synthase determined by nmr spectroscopy
    • Wilkens, S., Dahlquist, F. M., McIntosh, L. P., Donaldson, L. W. and Capaldi, R. A. (1995). Structural features of the ε 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.M.2    McIntosh, L.P.3    Donaldson, L.W.4    Capaldi, R.A.5
  • 48
    • 0028067602 scopus 로고
    • 0 ATP synthase: Effect of position 61 substitutions in helix-2 on function of Asp24 in helix-1
    • 0 ATP synthase: Effect of position 61 substitutions in helix-2 on function of Asp24 in helix-1. J. Biol. Chem. 269, 5473-5479.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5473-5479
    • Zhang, Y.1    Fillingame, R.H.2
  • 49
    • 0028800799 scopus 로고
    • +-transporting ATP synthase by directed mutagenesis of subunit c
    • +-transporting ATP synthase by directed mutagenesis of subunit c. J. Biol. Chem. 270, 87-93.
    • (1995) J. Biol. Chem. , vol.270 , pp. 87-93
    • Zhang, Y.1    Fillingame, R.H.2


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