메뉴 건너뛰기




Volumn 261, Issue 2, 1999, Pages 459-467

NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles

Author keywords

ATP synthase; NMR structure; Propionigenium modestum; Subunit c

Indexed keywords

DODECYL SULFATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SODIUM ION;

EID: 0033560680     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00288.x     Document Type: Article
Times cited : (43)

References (63)
  • 4
    • 0031016071 scopus 로고    scopus 로고
    • Primary sodium ion translocating enzymes
    • 4. Dimroth, P. (1997) Primary sodium ion translocating enzymes. Biochim. Biophys. Acta 1318, 11-51.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 11-51
    • Dimroth, P.1
  • 6
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthasesome probabilities and possibilities
    • 6. Boyer, P.D. (1993) The binding change mechanism for ATP synthasesome probabilities and possibilities. Biochim. Biophys. Acta 1140, 215-250.
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 9
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • 9. Sabbert, D., Engelbrecht, S. & 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
  • 14
    • 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
  • 16
    • 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
  • 17
    • 0028844612 scopus 로고
    • +-coupled ATP synthesis in the Escherichia coli host cells
    • +-coupled ATP synthesis in the Escherichia coli host cells. J. Mol. Biol. 253, 726-738.
    • (1995) J. Mol. Biol. , vol.253 , pp. 726-738
    • Kaim, G.1    Dimroth, P.2
  • 19
    • 0032531926 scopus 로고    scopus 로고
    • Voltage-generated torque drives the motor of the ATP synthase
    • 19. Kaim, G. & Dimroth, P. (1998) Voltage-generated torque drives the motor of the ATP synthase. EMBO J. 17, 5887-5895.
    • (1998) EMBO J. , vol.17 , pp. 5887-5895
    • Kaim, G.1    Dimroth, P.2
  • 20
    • 0031596006 scopus 로고    scopus 로고
    • 0 ATP synthase of Escherichia coli is obligatorily dependent on the electric potential
    • 0 ATP synthase of Escherichia coli is obligatorily dependent on the electric potential. FEBS Lett. 434, 57-60.
    • (1998) FEBS Lett. , vol.434 , pp. 57-60
    • Kaim, G.1    Dimroth, P.2
  • 22
    • 0032576724 scopus 로고    scopus 로고
    • Energy transduction in ATP synthase
    • 22. Elston, T., Wang, H. & 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
  • 23
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrical transducer with rotary mechanics
    • 23. Junge, W., Lill, H. & Engelbrecht, S. (1997) ATP synthase: an electrical transducer with rotary 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
  • 24
    • 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
  • 26
    • 0030851913 scopus 로고    scopus 로고
    • 0-ATPase of Propionigenium modestum. Production, purification and properties of the protein in dodecylsulfate solution
    • 0-ATPase of Propionigenium modestum. Production, purification and properties of the protein in dodecylsulfate solution. Eur. J. Biochem. 247, 820-825.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 820-825
    • Matthey, U.1    Kaim, G.2    Dimroth, P.3
  • 27
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling: Application to the study of hydrogen exchange proteins
    • 27. Marion, D., Ikura, M., Tschudin, R. & Bax, A. (1989) Rapid recording of 2D NMR spectra without phase cycling: application to the study of hydrogen exchange proteins. J. Magn. Reson. 85, 393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 28
    • 0001594959 scopus 로고
    • Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients
    • 28. Bax, A. & Pochapsky, S.S. (1992) Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients. J. Magn. Reson. 99, 638-643.
    • (1992) J. Magn. Reson. , vol.99 , pp. 638-643
    • Bax, A.1    Pochapsky, S.S.2
  • 29
    • 43949164434 scopus 로고
    • A simple experimental scheme using pulse field gradients for coherence-pathway rejection and solvent suppression in phase-sensitive heteronuclear correlation spectra
    • 29. Wider, G. & Wüthrich, K. (1993) A simple experimental scheme using pulse field gradients for coherence-pathway rejection and solvent suppression in phase-sensitive heteronuclear correlation spectra. J. Magn. Reson. B 102, 239-241.
    • (1993) J. Magn. Reson. B , vol.102 , pp. 239-241
    • Wider, G.1    Wüthrich, K.2
  • 30
    • 44949282610 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy
    • 30. Cavanagh, J., Palmer, A.G. III, Wright, P.E. & Rance, M. (1991) Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy. J. Magn. Reson. 91, 429-436.
    • (1991) J. Magn. Reson. , vol.91 , pp. 429-436
    • Cavanagh, J.1    Palmer A.G. III2    Wright, P.E.3    Rance, M.4
  • 31
    • 0000088628 scopus 로고
    • Processing of multi-dimensional NMR data with the new software PROSA
    • 31. Güntert, P., Dötsch, V., Wider, G. & Wüthrich, K. (1992) Processing of multi-dimensional NMR data with the new software PROSA. J. Biomol. NMR 2, 619-629.
    • (1992) J. Biomol. NMR , vol.2 , pp. 619-629
    • Güntert, P.1    Dötsch, V.2    Wider, G.3    Wüthrich, K.4
  • 32
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • 32. Bartels, C., Xia, T., Billeter, M., Güntert, P. & Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biol. NMR 6, 1-10.
    • (1995) J. Biol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 33
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 33. Koradi, R., Billeter, M. & Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 36
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113, 5490-5492.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 40
    • 0027483741 scopus 로고
    • 1H NMR resonance assignments and NOE analysis
    • 1H NMR resonance assignments and NOE analysis. Biochemistry 32, 12167-12177.
    • (1993) Biochemistry , vol.32 , pp. 12167-12177
    • Girvin, M.E.1    Fillingame, R.H.2
  • 41
    • 0028044903 scopus 로고
    • 1H distance measurements to nitroxide-derivatized aspartyl-61
    • 1H distance measurements to nitroxide-derivatized aspartyl-61. Biochemistry 33, 665-674.
    • (1994) Biochemistry , vol.33 , pp. 665-674
    • Girvin, M.E.1    Fillingame, R.H.2
  • 44
    • 0024293219 scopus 로고
    • Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump
    • 44. Laubinger, W. & Dimroth, P. (1988) Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump. Biochemistry 27, 7531-7537.
    • (1988) Biochemistry , vol.27 , pp. 7531-7537
    • Laubinger, W.1    Dimroth, P.2
  • 46
    • 0024277334 scopus 로고
    • 0 part of the ATP synthase from Escherichia coli. Influence of subunits a, and b, on the structure of subunit c
    • 0 part of the ATP synthase from Escherichia coli. Influence of subunits a, and b, on the structure of subunit c. Eur. J. Biochem. 170, 627-630.
    • (1988) Eur. J. Biochem. , vol.170 , pp. 627-630
    • Steffens, K.1    Hoppe, J.2    Altendorf, K.3
  • 48
    • 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
  • 49
    • 0018118592 scopus 로고
    • Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 49. Richarz, R. & Wüthrich, K. (1978) Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear telrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 17, 2133-2141.
    • (1978) Biopolymers , vol.17 , pp. 2133-2141
    • Richarz, R.1    Wüthrich, K.2
  • 50
    • 84985733652 scopus 로고
    • 1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 18, 285-297.
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 51
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • 51. Kyte, J. & Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 52
  • 54
    • 0000911456 scopus 로고
    • Multidimensional NMR experiments with improved resolution
    • 54. Madsen, J.C. & Sørensen, O.W. (1992) Multidimensional NMR experiments with improved resolution. J. Magn. Res. 100, 431-436.
    • (1992) J. Magn. Res. , vol.100 , pp. 431-436
    • Madsen, J.C.1    Sørensen, O.W.2
  • 55
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • 55. Grzesiek, S. & Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114, 6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 58
    • 0025374145 scopus 로고
    • Proton-proton correlation via carbon-carbon couplings: A three dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13
    • 58. Kay, L.E., Ikura, M. & Bax, A. (1990) Proton-proton correlation via carbon-carbon couplings: a three dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13. J. Am. Chem. Soc. 112, 888-889.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 888-889
    • Kay, L.E.1    Ikura, M.2    Bax, A.3
  • 59
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • 59. Kumar, A., Ernst, R.R. & Wüthrich, K. (1980) A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 60
    • 0000470905 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra
    • 60. Fesik, S.W. & Zuiderweg, E.R.P. (1988) Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra. J. Magn. Reson. 78, 588-593.
    • (1988) J. Magn. Reson. , vol.78 , pp. 588-593
    • Fesik, S.W.1    Zuiderweg, E.R.P.2
  • 62
    • 0025924784 scopus 로고
    • 13C-edited nuclear overhauser enhancement spectroscopy of a protein in solution: Application to interleukin Iβ
    • 13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin Iβ. Biochemistry 30, 12-18.
    • (1991) Biochemistry , vol.30 , pp. 12-18
    • Clore, G.M.1    Kay, L.E.2    Bax, A.3    Gronenborn, A.G.4
  • 63
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115, 12593-12594.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.