메뉴 건너뛰기




Volumn 132, Issue 5, 2002, Pages 789-794

Nucleotide-binding sites in V-type Na+-ATPase from Enterococcus hirae

Author keywords

Enterococcus hirae; Homology modeling; Na+ translocating ATPase; Nucleotide binding; V ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATASE; N ETHYLMALEIMIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SODIUM; THIOL REAGENT;

EID: 0036855440     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003288     Document Type: Article
Times cited : (6)

References (35)
  • 1
    • 0025338413 scopus 로고
    • The proton-translocating ATPase of Escherichia coli
    • Senior, A. E. (1990) The proton-translocating ATPase of Escherichia coli. Ann. Rev. Biopys. Chem. 19, 7-41
    • (1990) Ann. Rev. Biopys. Chem. , vol.19 , pp. 7-41
    • Senior, A.E.1
  • 4
    • 0024354291 scopus 로고
    • +ATPase): Results by combined biochemical and molecular biological approaches
    • +ATPase): Results by combined biochemical and molecular biological approaches. Ann. Rev. Biochem. 58, 111-136
    • (1989) Ann. Rev. Biochem. , vol.58 , pp. 111-136
    • Futai, M.1    Noumi, T.2    Maeda, M.3
  • 5
    • 0031452168 scopus 로고    scopus 로고
    • Structure, function and regulation of the vacuolar (H-)-ATPase
    • Stevens, T.H. and Forgac, M. (1997) Structure, function and regulation of the vacuolar (H-)-ATPase. Annu. Rev. Cell Dev. Biol. 13, 779-808
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 779-808
    • Stevens, T.H.1    Forgac, M.2
  • 7
    • 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
  • 8
    • 0033609081 scopus 로고    scopus 로고
    • Energy transduction in the sodium F-ATPase of Propionigenium modestum
    • Dimroth, P., Wang, H., Grabe, M., and Oster, G. (1999) Energy transduction in the sodium F-ATPase of Propionigenium modestum. Proc. Natl. Acad. Sci. USA 96, 4924-4929
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4924-4929
    • Dimroth, P.1    Wang, H.2    Grabe, M.3    Oster, G.4
  • 10
    • 0024389333 scopus 로고
    • Structure and function of the vacuolar class of ATP-driven proton pumps
    • Forgac, M. (1989) Structure and function of the vacuolar class of ATP-driven proton pumps. Physiol. Rev. 69, 765-796
    • (1989) Physiol. Rev. , vol.69 , pp. 765-796
    • Forgac, M.1
  • 11
    • 0034614422 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis of the noncatalytic nucleotide binding site of the yeast V-ATPase
    • Vasilyeva, E., Liu, Q., Macleod, K.J., Baleja, J.D., and Forgac, M. (2000) Cysteine scanning mutagenesis of the noncatalytic nucleotide binding site of the yeast V-ATPase. J. Biol. Chem. 275, 255-260
    • (2000) J. Biol. Chem. , vol.275 , pp. 255-260
    • Vasilyeva, E.1    Liu, Q.2    Macleod, K.J.3    Baleja, J.D.4    Forgac, M.5
  • 18
    • 0023494785 scopus 로고
    • Detection of weak sequence homology of proteins for tertiary structure prediction
    • Nishikawa, K., Nakashima, H., Kanehisa, M., and Ooi, M. (1987) Detection of weak sequence homology of proteins for tertiary structure prediction. Protein Seq. Data Anal. 1, 107-116
    • (1987) Protein Seq. Data Anal. , vol.1 , pp. 107-116
    • Nishikawa, K.1    Nakashima, H.2    Kanehisa, M.3    Ooi, M.4
  • 19
    • 0025882349 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch, A. (1991) PROSITE: A dictionary of sites and patterns in proteins. Nucleic Acids Res. 19, 2241-2245
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2241-2245
    • Bairoch, A.1
  • 20
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins, D.G., Bleasby, A. J., and Fuchs, R. (1992) CLUSTAL V: Improved software for multiple sequence alignment. Comput. Appl. Biosci. 8, 189-191
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 24
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R., Bowie, J.U., and Eisenberg, D. (1992) Assessment of protein models with three-dimensional profiles. Nature 356, 83-85
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 25
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B. and Nicholls, A. (1995) Classical electrostatics in biology and chemistry. Science 268, 1144-1149
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 27
    • 0026688602 scopus 로고
    • +ATPase upon modification by sulfhydryl reagents
    • +ATPase upon modification by sulfhydryl reagents. J. Biol. Chem. 267, 5817-5822
    • (1992) J. Biol. Chem. , vol.267 , pp. 5817-5822
    • Feng, Y.1    Forgac, M.2
  • 30
    • 0025145055 scopus 로고
    • +-ATPase resemble those of vacuolar-type ATPases
    • +- ATPase resemble those of vacuolar-type ATPases. FEBS Lett. 271, 97-101
    • (1990) FEBS Lett. , vol.271 , pp. 97-101
    • Kakinuma, Y.1    Igarashi, K.2
  • 31
    • 0032493661 scopus 로고    scopus 로고
    • V-ATPase of Thermus thermophilus is inactivated during ATP hydrolysis but can synthesize ATP
    • Yokoyama, K., Muneyuki, E., Amano, T., Mizutani, S., Yoshida, M., Ishida, M., and Ohkuma, S. (1998) V-ATPase of Thermus thermophilus is inactivated during ATP hydrolysis but can synthesize ATP. J. Biol. Chem. 273, 20504-20510
    • (1998) J. Biol. Chem. , vol.273 , pp. 20504-20510
    • Yokoyama, K.1    Muneyuki, E.2    Amano, T.3    Mizutani, S.4    Yoshida, M.5    Ishida, M.6    Ohkuma, S.7
  • 32
    • 0029946927 scopus 로고    scopus 로고
    • +ATPase from bovine brain clathrin-coated vesicles by modification of a rapidly exchangeable, noncatalytic nucleotide binding site on the B subunit
    • +ATPase from bovine brain clathrin-coated vesicles by modification of a rapidly exchangeable, noncatalytic nucleotide binding site on the B subunit. J. Biol. Chem. 271, 12775-12782
    • (1996) J. Biol. Chem. , vol.271 , pp. 12775-12782
    • Vasilyeva, E.1    Forgac, M.2
  • 34
    • 0029040432 scopus 로고
    • Nucleotide labeling and reconstitution of the recombinant 58-kDa subunit of the vacuolar proton-translocating ATPase
    • Peng, S.-B. (1995) Nucleotide labeling and reconstitution of the recombinant 58-kDa subunit of the vacuolar proton-translocating ATPase. J. Biol. Chem. 270, 16926-16931
    • (1995) J. Biol. Chem. , vol.270 , pp. 16926-16931
    • Peng, S.-B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.