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Volumn 267, Issue 4, 2000, Pages 1008-1018

High resolution solution structure of the protein part of Cu7 metallothionein

Author keywords

Cu7 metallothionein; NMR protein structure; Yeast

Indexed keywords

METALLOTHIONEIN;

EID: 0033955655     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01093.x     Document Type: Article
Times cited : (46)

References (39)
  • 1
    • 0023087396 scopus 로고
    • Chemistry and biochemistry of metallothionein
    • 1. Kaegi, J.H.R. & Kojima, Y. (1987) Chemistry and biochemistry of metallothionein. Experientia Suppl. 52, 25-61.
    • (1987) Experientia Suppl. , vol.52 , pp. 25-61
    • Kaegi, J.H.R.1    Kojima, Y.2
  • 2
    • 0000119940 scopus 로고
    • Structure of the metal clusters in rabbit liver metallo-thionein
    • 2. Otvos, J.D. & Armitage, I.M. (1980) Structure of the metal clusters in rabbit liver metallo-thionein. Proc. Natl Acad. Sci. USA 77, 7094-7098.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 7094-7098
    • Otvos, J.D.1    Armitage, I.M.2
  • 3
    • 0020478923 scopus 로고
    • Domain nature of metallo-thionein
    • 3. Winge, D.R. & Miklossy, K.-A. (1982) Domain nature of metallo-thionein. J. Biol. Chem. 257, 3471-3476.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3471-3476
    • Winge, D.R.1    Miklossy, K.-A.2
  • 4
    • 0021356888 scopus 로고
    • Preferential binding of copper to the β-domain of metallothionein
    • 4. Nielson, K.B. & Winge, D.R. (1984) Preferential binding of copper to the β-domain of metallothionein. J. Biol. Chem. 259, 4941-4946.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4941-4946
    • Nielson, K.B.1    Winge, D.R.2
  • 5
    • 0023073046 scopus 로고
    • Information on metal binding properties of metallothioneins from optical spectroscopy
    • 5. Stillman, M.J., Law, A.J.C., Cai, W. & Zelazowski, A.J. (1987) Information on metal binding properties of metallothioneins from optical spectroscopy. Experientia Suppl. 52, 203-211.
    • (1987) Experientia Suppl. , vol.52 , pp. 203-211
    • Stillman, M.J.1    Law, A.J.C.2    Cai, W.3    Zelazowski, A.J.4
  • 6
    • 0001571168 scopus 로고
    • Circular dichroism, luminescence and electronic absorption of copper binding sites in metallothionein and its chemically synthesized α- and β-domains
    • 6. Li, Y.-J. & Weser, U. (1992) Circular dichroism, luminescence and electronic absorption of copper binding sites in metallothionein and its chemically synthesized α-and β-domains. Inorg. Chem. 31, 5526-5533.
    • (1992) Inorg. Chem. , vol.31 , pp. 5526-5533
    • Li, Y.-J.1    Weser, U.2
  • 7
    • 0016805880 scopus 로고
    • A naturally occurring Cu-thionein in Saccharomyces cerevisiae
    • 7. Prinz, R. & Weser, U. (1975) A naturally occurring Cu-thionein in Saccharomyces cerevisiae. Hoppe-Seyler's Z. Physiol. Chem. 356, 767-776.
    • (1975) Hoppe-Seyler's Z. Physiol. Chem. , vol.356 , pp. 767-776
    • Prinz, R.1    Weser, U.2
  • 8
    • 0022432526 scopus 로고
    • Yeast metallothionein. Sequence and metal-binding properties
    • 8. Winge, D.R., Nielson, D.B., Gray, W.R. & Hamer, D.H. (1985) Yeast metallothionein. Sequence and metal-binding properties. J. Biol. Chem. 260, 14464-14470.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14464-14470
    • Winge, D.R.1    Nielson, D.B.2    Gray, W.R.3    Hamer, D.H.4
  • 9
    • 0026317899 scopus 로고
    • Purification of yeast Cu-thioncin
    • 9. Weser, U. & Hartmann, H.-J. (1991) Purification of yeast Cu-thioncin. Methods Enzymol. 205, 274-278.
    • (1991) Methods Enzymol. , vol.205 , pp. 274-278
    • Weser, U.1    Hartmann, H.-J.2
  • 11
    • 0024287598 scopus 로고
    • Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants
    • 11. Byrd, J., Berger, R.M., McMillin, D.R., Wright, C.F., Hamer, D.H. & Winge, D.R. (1988) Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants. J. Biol. Chem. 263, 6688-6694.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6688-6694
    • Byrd, J.1    Berger, R.M.2    McMillin, D.R.3    Wright, C.F.4    Hamer, D.H.5    Winge, D.R.6
  • 12
    • 0023917462 scopus 로고
    • X-ray absorption studies of yeast copper metallothionein
    • 12. George, G.N., Byrd, J. & Winge, D.R. (1988) X-ray absorption studies of yeast copper metallothionein. J. Biol. Chem. 263, 8199-8203.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8199-8203
    • George, G.N.1    Byrd, J.2    Winge, D.R.3
  • 13
    • 0024275854 scopus 로고
    • Differently bound copper (I) in yeast Cu-thionein
    • 13. Weser, U. & Hartmann, H.-J. (1988) Differently bound copper (I) in yeast Cu-thionein. Biochim. Biophys. Acta 953, 1-5.
    • (1988) Biochim. Biophys. Acta , vol.953 , pp. 1-5
    • Weser, U.1    Hartmann, H.-J.2
  • 14
    • 0026927997 scopus 로고
    • Analogous copper (I) coordination in metallothionein from yeast and the separate domains of the mammalian protein
    • 14. Hartmann, H.-J., Li, Y.-J. & Weser, U. (1992) Analogous copper (I) coordination in metallothionein from yeast and the separate domains of the mammalian protein. Biometals 5, 187-191.
    • (1992) Biometals , vol.5 , pp. 187-191
    • Hartmann, H.-J.1    Li, Y.-J.2    Weser, U.3
  • 16
    • 0343299702 scopus 로고
    • Tandem gene amplification mediates copper resistance in yeast
    • 16. Fogel, S. & Welch, J.W. (1982) Tandem gene amplification mediates copper resistance in yeast. Proc. Natl Acad. Sci. USA 79, 5342-5346.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 5342-5346
    • Fogel, S.1    Welch, J.W.2
  • 17
    • 0021839915 scopus 로고
    • Function and autoregulation of yeast copper thionein
    • 17. Hamer, D.H., Thiele, D.J. & Lemontt, J. (1985) Function and autoregulation of yeast copper thionein. Science 288, 685-690.
    • (1985) Science , vol.288 , pp. 685-690
    • Hamer, D.H.1    Thiele, D.J.2    Lemontt, J.3
  • 20
    • 0023937834 scopus 로고
    • Three-dimensional structure of rabbit liver Cd-metallothionein-2a in aqueous solution determined by nuclear magnetic resonance
    • 20. Arseniev, A., Schultze, P., Wörgötter, E., Braun, W., Wagner, G., Vasak, M., Kägi, J.H.R. & Wüthrich, K. (1988) Three-dimensional structure of rabbit liver Cd-metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J. Mol. Biol. 201, 637-657.
    • (1988) J. Mol. Biol. , vol.201 , pp. 637-657
    • Arseniev, A.1    Schultze, P.2    Wörgötter, E.3    Braun, W.4    Wagner, G.5    Vasak, M.6    Kägi, J.H.R.7    Wüthrich, K.8
  • 21
    • 0030052073 scopus 로고    scopus 로고
    • 3D solution structure of copper and silver-substituted yeast metallothioneins
    • 21. Peterson, C.W., Narula, S.S. & Armitage, I.M. (1996) 3D solution structure of copper and silver-substituted yeast metallothioneins. FEBS Lett. 379, 85-93.
    • (1996) FEBS Lett. , vol.379 , pp. 85-93
    • Peterson, C.W.1    Narula, S.S.2    Armitage, I.M.3
  • 22
    • 0000204980 scopus 로고
    • Establishment of the metal-to-cysteine connectivities in silver-substituted yeast metallothionein
    • 22. Narula, S.S., Mehra, R.K., Winge, D.R. & Armitage, I.M. (1991) Establishment of the metal-to-cysteine connectivities in silver-substituted yeast metallothionein. J. Am. Chem. Soc. 113, 9354-9358.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9354-9358
    • Narula, S.S.1    Mehra, R.K.2    Winge, D.R.3    Armitage, I.M.4
  • 23
    • 0027321313 scopus 로고
    • 1H NMR assignment reflecting conformational heterogeneity at the C terminus
    • 1H NMR assignment reflecting conformational heterogeneity at the C terminus. Biochemistry 32, 6773-6787.
    • (1993) Biochemistry , vol.32 , pp. 6773-6787
    • Narula, S.S.1    Winge, D.R.2    Armitage, I.M.3
  • 25
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solutions
    • 25. Piotto, M., Saudek, V. & Sklenar, V. (1992) Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-666.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-666
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 26
    • 0000849756 scopus 로고
    • The relevance of J cross-peaks in two-dimensional NOE experiments of macro-molecules
    • 26. Macura, S., Wüthrich, K. & Ernst, R.R. (1982) The relevance of J cross-peaks in two-dimensional NOE experiments of macro-molecules. J. Magn. Reson. 47, 351-357.
    • (1982) J. Magn. Reson. , vol.47 , pp. 351-357
    • Macura, S.1    Wüthrich, K.2    Ernst, R.R.3
  • 27
    • 0021114895 scopus 로고
    • Application of phase sensitive correlated spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins
    • 27. Marion, D. & Wüthrich, K. (1983) Application of phase sensitive correlated spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113, 967-974.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 28
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • 28. Bax, A. & Davis, D.G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 29
    • 0026193519 scopus 로고
    • Efficient analysis of protein 2D NMR spectra using the software package EASY
    • 29. Eccles, C., Güntert, P., Billeter, M. & Wüthrich, K. (1991) Efficient analysis of protein 2D NMR spectra using the software package EASY. J. Biomol. NMR 1, 111-130.
    • (1991) J. Biomol. NMR , vol.1 , pp. 111-130
    • Eccles, C.1    Güntert, P.2    Billeter, M.3    Wüthrich, K.4
  • 30
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • 30. Güntert, P., Braun, W. & Wüthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from Nuclear Magnetic Resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217, 517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 31
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • 31. Güntert, P., Mumenthaler, C. & Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 33
    • 0004240394 scopus 로고
    • University of California, San Francisco
    • 33. Pearlman, D.A. & Case, D.A. (1991) SANDER: University of California, San Francisco.
    • (1991) SANDER
    • Pearlman, D.A.1    Case, D.A.2
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 35. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 36
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structure
    • 36. Koradi, R., Billeter, M. & Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structure. J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


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