메뉴 건너뛰기




Volumn 274, Issue 9, 2007, Pages 2349-2362

Coordination of three and four Cu(I) to the α- and β-domain of vertebrate Zn-metallothionein-1, respectively, induces significant structural changes

Author keywords

2D NMR; Copper; Domain; Metallothionein; Protein structure

Indexed keywords

COPPER ION; METALLOTHIONEIN I; ZINC;

EID: 34247326875     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05770.x     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 0001593597 scopus 로고
    • Metallothionein: A cadmium- and zinc-containing protein from equine renal cortex
    • Kagi JH Vallee BL (1960) Metallothionein: a cadmium- and zinc-containing protein from equine renal cortex. J Biol Chem 235, 3460 3465.
    • (1960) J Biol Chem , vol.235 , pp. 3460-3465
    • Kagi, J.H.1    Vallee, B.L.2
  • 2
    • 0023087396 scopus 로고
    • Chemistry and biochemistry of metallothionein
    • Kagi JH Kojima Y (1987) Chemistry and biochemistry of metallothionein. Experientia Suppl 52, 25 61.
    • (1987) Experientia Suppl , vol.52 , pp. 25-61
    • Kagi, J.H.1    Kojima, Y.2
  • 3
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter RD (1998) The elusive function of metallothioneins. Proc Natl Acad Sci USA 95, 8428 8430.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 4
    • 0027486416 scopus 로고
    • A pulse radiolytic study on the reaction of hydroxyl and superoxide radicals with yeast Cu(I)-thionein
    • Felix K, Lengfelder E, Hartmann HJ Weser U (1993) A pulse radiolytic study on the reaction of hydroxyl and superoxide radicals with yeast Cu(I)-thionein. Biochim Biophys Acta 1203, 104 108.
    • (1993) Biochim Biophys Acta , vol.1203 , pp. 104-108
    • Felix, K.1    Lengfelder, E.2    Hartmann, H.J.3    Weser, U.4
  • 5
    • 0021944046 scopus 로고
    • Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals
    • Thornalley PJ Vasak M (1985) Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals. Biochim Biophys Acta 827, 36 44.
    • (1985) Biochim Biophys Acta , vol.827 , pp. 36-44
    • Thornalley, P.J.1    Vasak, M.2
  • 6
    • 0028263925 scopus 로고
    • Enhanced neurotrophic activity in Alzheimer's disease cortex is not associated with down-regulation of metallothionein-III (GIF)
    • Erickson JC, Sewell AK, Jensen LT, Winge DR Palmiter RD (1994) Enhanced neurotrophic activity in Alzheimer's disease cortex is not associated with down-regulation of metallothionein-III (GIF). Brain Res 649, 297 304.
    • (1994) Brain Res , vol.649 , pp. 297-304
    • Erickson, J.C.1    Sewell, A.K.2    Jensen, L.T.3    Winge, D.R.4    Palmiter, R.D.5
  • 7
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
    • Uchida Y, Takio K, Titani K, Ihara Y Tomonaga M (1991) The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein. Neuron 7, 337 347.
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 8
    • 0036189730 scopus 로고    scopus 로고
    • Advances in the structure and chemistry of metallothioneins
    • Romero-Isart N Vasak M (2002) Advances in the structure and chemistry of metallothioneins. J Inorg Biochem 88, 388 396.
    • (2002) J Inorg Biochem , vol.88 , pp. 388-396
    • Romero-Isart, N.1    Vasak, M.2
  • 9
    • 0017361007 scopus 로고
    • Copper-thionein from fetal bovine liver
    • Hartmann HJ Weser U (1977) Copper-thionein from fetal bovine liver. Biochim Biophys Acta 491, 211 222.
    • (1977) Biochim Biophys Acta , vol.491 , pp. 211-222
    • Hartmann, H.J.1    Weser, U.2
  • 10
    • 0036941677 scopus 로고    scopus 로고
    • A distinct Cu(4)-thiolate cluster of human metallothionein-3 is located in the N-terminal domain
    • Roschitzki B Vasak M (2002) A distinct Cu(4)-thiolate cluster of human metallothionein-3 is located in the N-terminal domain. J Biol Inorg Chem 7, 611 616.
    • (2002) J Biol Inorg Chem , vol.7 , pp. 611-616
    • Roschitzki, B.1    Vasak, M.2
  • 11
    • 0041525416 scopus 로고    scopus 로고
    • Redox labile site in a Zn4 cluster of Cu4,Zn4-metallothionein-3
    • Roschitzki B Vasak M (2003) Redox labile site in a Zn4 cluster of Cu4,Zn4-metallothionein-3. Biochemistry 42, 9822 9828.
    • (2003) Biochemistry , vol.42 , pp. 9822-9828
    • Roschitzki, B.1    Vasak, M.2
  • 12
    • 0016805880 scopus 로고
    • A naturally occurring Cu-thionein in Saccharomyces cerevisiae
    • Prinz R Weser U (1975) A naturally occurring Cu-thionein in Saccharomyces cerevisiae. Hoppe Seylers Z Physiol Chem 356, 767 776.
    • (1975) Hoppe Seylers Z Physiol Chem , vol.356 , pp. 767-776
    • Prinz, R.1    Weser, U.2
  • 13
    • 0024287598 scopus 로고
    • Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants
    • Byrd J, Berger RM, McMillin DR, Wright CF, Hamer D Winge DR (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.5    Winge, D.R.6
  • 14
    • 0022560382 scopus 로고
    • Primary structure and spectroscopic studies of Neurospora copper metallothionein
    • Beltramini M Lerch K (1986) Primary structure and spectroscopic studies of Neurospora copper metallothionein. Environ Health Perspect 65, 21 27.
    • (1986) Environ Health Perspect , vol.65 , pp. 21-27
    • Beltramini, M.1    Lerch, K.2
  • 16
    • 0026647117 scopus 로고
    • Comparison of the solution conformations of human [zn7]-metallothionein-2 and [cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy
    • Messerle BA, Schaffer A, Vasak M, Kagi JH Wuthrich K (1992) Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy. J Mol Biol 225, 433 443.
    • (1992) J Mol Biol , vol.225 , pp. 433-443
    • Messerle, B.A.1    Schaffer, A.2    Vasak, M.3    Kagi, J.H.4    Wuthrich, K.5
  • 17
    • 0024426560 scopus 로고
    • Proton NMR studies of the cobalt(II)-metallothionein system
    • Bertini I, Luchinat C, Messori L Vasak M (1989) Proton NMR studies of the cobalt(II)-metallothionein system. J Am Chem Soc 111, 7296 7300.
    • (1989) J Am Chem Soc , vol.111 , pp. 7296-7300
    • Bertini, I.1    Luchinat, C.2    Messori, L.3    Vasak, M.4
  • 18
    • 0024447648 scopus 로고
    • Proton NMR spectra of the Co4S11 cluster in metallothioneins: A theoretical model
    • Bertini I, Luchinat C, Messori L Vasak M (1989) Proton NMR spectra of the Co4S11 cluster in metallothioneins: a theoretical model. J Am Chem Soc 111, 7300 7303.
    • (1989) J Am Chem Soc , vol.111 , pp. 7300-7303
    • Bertini, I.1    Luchinat, C.2    Messori, L.3    Vasak, M.4
  • 19
    • 0027518283 scopus 로고
    • A two-dimensional NMR study of Co(II)7 rabbit liver metallothionein
    • Bertini I, Luchinat C, Messori L Vasak M (1993) A two-dimensional NMR study of Co(II)7 rabbit liver metallothionein. Eur J Biochem 211, 235 240.
    • (1993) Eur J Biochem , vol.211 , pp. 235-240
    • Bertini, I.1    Luchinat, C.2    Messori, L.3    Vasak, M.4
  • 20
    • 0342614962 scopus 로고    scopus 로고
    • Three-dimensional solution structure of mouse [cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy
    • Zangger K, Oz G, Otvos JD Armitage IM (1999) Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy. Protein Sci 8, 2630 2638.
    • (1999) Protein Sci , vol.8 , pp. 2630-2638
    • Zangger, K.1    Oz, G.2    Otvos, J.D.3    Armitage, I.M.4
  • 21
    • 0035949634 scopus 로고    scopus 로고
    • Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: Metallothionein-3
    • Oz G, Zangger K Armitage IM (2001) Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: metallothionein-3. Biochemistry 40, 11433 11441.
    • (2001) Biochemistry , vol.40 , pp. 11433-11441
    • Oz, G.1    Zangger, K.2    Armitage, I.M.3
  • 22
    • 0033955655 scopus 로고    scopus 로고
    • High resolution solution structure of the protein part of Cu7 metallothionein
    • Bertini I, Hartmann HJ, Klein T, Liu G, Luchinat C Weser U (2000) High resolution solution structure of the protein part of Cu7 metallothionein. Eur J Biochem 267, 1008 1018.
    • (2000) Eur J Biochem , vol.267 , pp. 1008-1018
    • Bertini, I.1    Hartmann, H.J.2    Klein, T.3    Liu, G.4    Luchinat, C.5    Weser, U.6
  • 23
    • 0030052073 scopus 로고    scopus 로고
    • 3D solution structure of copper and silver-substituted yeast metallothioneins
    • Peterson CW, Narula SS Armitage IM (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
  • 26
    • 0001571168 scopus 로고
    • Circular dichroism, luminescence, and electronic absorption of copper binding sites in metallothionein and its chemically synthesized α and β domains
    • Li YJ 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
  • 27
    • 0034852792 scopus 로고    scopus 로고
    • Zinc (II) is required for the in vivo and in vitro folding of mouse copper metallothionein in two domains
    • Bofill R, Capdevila M, Cols N, Atrian S Gonzalez-Duarte P (2001) Zinc (II) is required for the in vivo and in vitro folding of mouse copper metallothionein in two domains. J Biol Inorg Chem 6, 405 417.
    • (2001) J Biol Inorg Chem , vol.6 , pp. 405-417
    • Bofill, R.1    Capdevila, M.2    Cols, N.3    Atrian, S.4    Gonzalez-Duarte, P.5
  • 30
    • 0037081545 scopus 로고    scopus 로고
    • Copper speciation in the alpha and beta domains of recombinant human metallothionein by electrospray ionization mass spectrometry
    • Merrifield ME, Huang Z, Kille P Stillman MJ (2002) Copper speciation in the alpha and beta domains of recombinant human metallothionein by electrospray ionization mass spectrometry. J Inorg Biochem 88, 153 172.
    • (2002) J Inorg Biochem , vol.88 , pp. 153-172
    • Merrifield, M.E.1    Huang, Z.2    Kille, P.3    Stillman, M.J.4
  • 31
    • 0000849756 scopus 로고
    • The relevance of J cross-peaks in two-dimensional NOE experiments of macromolecules
    • Macura S, Wüthrich K Ernst RR (1982) The relevance of J cross-peaks in two-dimensional NOE experiments of macromolecules. 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
  • 32
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins
    • Marion D Wuthrich K (1983) Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H 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    Wuthrich, K.2
  • 33
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A Davis DG (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
  • 34
    • 0004757060 scopus 로고    scopus 로고
    • University of California, San Francisco, CA.
    • Goddard TD Kneller DG (2004) Sparky 3. University of California, San Francisco, CA.
    • (2004) Sparky , pp. 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 35
    • 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
    • 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
  • 36
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program dyana
    • 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
  • 37
    • 0029881007 scopus 로고    scopus 로고
    • Molmol: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M Wüthrich K (1996) molmol: a program for display and analysis of macromolecular structures. J Mol Graph 14, 51 32.
    • (1996) J Mol Graph , vol.14 , pp. 51-32
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.