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Volumn 365, Issue 2, 2008, Pages 227-231

Effects of mutations in the β subunit hinge domain on ATP synthase F1 sector rotation: Interaction between Ser 174 and Ile 163

Author keywords

Subunit; ATP synthase; ATPase; F1; Rotation; Ser 174

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALANINE; GLYCINE; ISOLEUCINE; PHENYLALANINE; PHOSPHATE; PHOSPHATE BINDING PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SERINE;

EID: 36249022248     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.157     Document Type: Article
Times cited : (10)

References (20)
  • 1
    • 84954271321 scopus 로고    scopus 로고
    • Proton-translocating ATPases: introducing unique enzymes coupling catalysis and proton translocation through mechanical rotation
    • Futai M., Wada Y., and Kaplan J. (Eds), Wiley-VCH Verlag, GmbH & Co. KGaA, Weinheim, Germany
    • Futai M., Sun-Wada G.H., and Wada Y. Proton-translocating ATPases: introducing unique enzymes coupling catalysis and proton translocation through mechanical rotation. In: Futai M., Wada Y., and Kaplan J. (Eds). Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology (2004), Wiley-VCH Verlag, GmbH & Co. KGaA, Weinheim, Germany 237-260
    • (2004) Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology , pp. 237-260
    • Futai, M.1    Sun-Wada, G.H.2    Wada, Y.3
  • 2
    • 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
  • 9
    • 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 (1998) 1117-1124
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinoshita Jr., K.3    Yoshida, M.4
  • 15
    • 0028339083 scopus 로고
    • +-ATPase (ATP synthase). An Escherichia coli α subunit mutation (Argα296→Cys) restores coupling efficiency to the deleterious β subunit mutant (Ser-β174→Phe)
    • +-ATPase (ATP synthase). An Escherichia coli α subunit mutation (Argα296→Cys) restores coupling efficiency to the deleterious β subunit mutant (Ser-β174→Phe). J. Biol. Chem. 269 (1994) 10265-10269
    • (1994) J. Biol. Chem. , vol.269 , pp. 10265-10269
    • Omote, H.1    Park, M.-Y.2    Maeda, M.3    Futai, M.4
  • 17
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 18
    • 14144256681 scopus 로고    scopus 로고
    • Energy functions for protein design: adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity
    • Pokala N., and Handel T.M. Energy functions for protein design: adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity. J. Mol. Biol. 347 (2005) 203-227
    • (2005) J. Mol. Biol. , vol.347 , pp. 203-227
    • Pokala, N.1    Handel, T.M.2
  • 19
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.-G., and Gibson T.J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.-G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.