메뉴 건너뛰기




Volumn 390, Issue 2, 2009, Pages 230-234

Modulation of nucleotide binding to the catalytic sites of thermophilic F1-ATPase by the ε subunit: Implication for the role of the ε subunit in ATP synthesis

Author keywords

Binding change mechanism; Epsilon subunit; F1 ATPase; Nucleotide binding; Regulation

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GUANOSINE DIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRYPTOPHAN;

EID: 70350130530     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.09.092     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase--a splendid molecular machine
    • Boyer P.D. The ATP synthase--a splendid molecular machine. Annu. Rev. Biochem. 66 (1997) 717-749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 7
    • 0018908352 scopus 로고
    • Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli
    • Sternweis P.C., and Smith J.B. Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli. Biochemistry 19 (1980) 526-531
    • (1980) Biochemistry , vol.19 , pp. 526-531
    • Sternweis, P.C.1    Smith, J.B.2
  • 9
    • 0028970620 scopus 로고
    • Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
    • Wilkens S., Dahlquist F.W., McIntosh L.P., Donaldson L.W., and Capaldi R.A. Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat. Struct. Biol. 2 (1995) 961-967
    • (1995) Nat. 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
  • 10
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli
    • Uhlin U., Cox G.B., and Guss J.M. Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli. Structure 5 (1997) 1219-1230
    • (1997) Structure , vol.5 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Guss, J.M.3
  • 11
    • 0033623349 scopus 로고    scopus 로고
    • Structure of the gamma-epsilon complex of ATP synthase
    • Rodgers A.J.W., and Wilce M.C.J. Structure of the gamma-epsilon complex of ATP synthase. Nat. Struct. Biol. 7 (2000) 1051-1054
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1051-1054
    • Rodgers, A.J.W.1    Wilce, M.C.J.2
  • 16
    • 0345306622 scopus 로고    scopus 로고
    • 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance
    • 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance. J. Biol. Chem. 278 (2003) 46840-46846
    • (2003) J. Biol. Chem. , vol.278 , pp. 46840-46846
    • Suzuki, T.1    Murakami, T.2    Iino, R.3    Suzuki, J.4    Ono, S.5    Shirakihara, Y.6    Yoshida, M.7
  • 20
    • 0023653176 scopus 로고
    • 1-ATPase: effect on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis
    • 1-ATPase: effect on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis. Biochemistry 26 (1987) 4488-4493
    • (1987) Biochemistry , vol.26 , pp. 4488-4493
    • Dunn, S.D.1    Zadorozny, V.D.2    Tozer, R.G.3    Orr, L.E.4
  • 28
    • 0034615699 scopus 로고    scopus 로고
    • 1-ATPase fro the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides
    • 1-ATPase fro the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides. J. Biol. Chem. 275 (2000) 10057-10063
    • (2000) J. Biol. Chem. , vol.275 , pp. 10057-10063
    • Ren, H.1    Allison, W.S.2
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0027317040 scopus 로고
    • 1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied
    • 1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied. J. Biol. Chem. 268 (1993) 20126-20133
    • (1993) J. Biol. Chem. , vol.268 , pp. 20126-20133
    • Weber, J.1    Wilke-Mounts, S.2    Lee, R.S.3    Grell, E.4    Senior, A.E.5
  • 35
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 106 (2001) 331-341
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.