메뉴 건너뛰기




Volumn 356, Issue 5, 2006, Pages 1152-1162

Variable metallation of human superoxide dismutase: Atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes

Author keywords

Atomic resolution structures; Catalysis; Copper zinc superoxide dismutase; Familial amyotrophic lateral sclerosis; SOD1

Indexed keywords

COPPER; SUPEROXIDE DISMUTASE; ZINC;

EID: 32044475396     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.11.081     Document Type: Article
Times cited : (151)

References (48)
  • 1
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn Superoxide-dismutase gene are associated with familial amyotrophic-lateral-sclerosis
    • D.R. Rosen, T. Siddique, D. Patterson, D.A. Figlewicz, P. Sapp, and A. Hentati Mutations in Cu/Zn Superoxide-dismutase gene are associated with familial amyotrophic-lateral-sclerosis Nature 362 1993 59 62
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3    Figlewicz, D.A.4    Sapp, P.5    Hentati, A.6
  • 2
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • J.S. Valentine, P.A. Doucette, and S.Z. Potter Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis Annu. Rev. Biochem. 74 2005 563 593
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Potter, S.Z.3
  • 3
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • D.W. Cleveland, and J.D. Rothstein From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS Nature Rev. Neurosci. 2 2001 806 819
    • (2001) Nature Rev. Neurosci. , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 4
    • 0037111503 scopus 로고    scopus 로고
    • Do oxidatively modified proteins cause ALS?
    • J.S. Valentine Do oxidatively modified proteins cause ALS? Free Radic. Biol. Med. 33 2001 1314 1320
    • (2001) Free Radic. Biol. Med. , vol.33 , pp. 1314-1320
    • Valentine, J.S.1
  • 5
    • 0037388067 scopus 로고    scopus 로고
    • Misfolded CuZnSOD and amyotrophic lateral sclerosis
    • J.S. Valentine, and P.J. Hart Misfolded CuZnSOD and amyotrophic lateral sclerosis Proc. Natl Acad. Sci. USA 100 2003 3617 3622
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 3617-3622
    • Valentine, J.S.1    Hart, P.J.2
  • 6
    • 16044366720 scopus 로고    scopus 로고
    • Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein
    • T.J. Lyons, H. Liu, J.J. Goto, A. Nersissian, J.A. Roe, and J.A. Graden Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein Proc. Natl Acad. Sci. USA 93 1996 12240 12244
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12240-12244
    • Lyons, T.J.1    Liu, H.2    Goto, J.J.3    Nersissian, A.4    Roe, J.A.5    Graden, J.A.6
  • 7
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • J.P. Crow, J.B. Sampson, Y.X. Zhuang, J.A. Thompson, and J.S. Beckman Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite J. Neurochem. 69 1997 1936 1944
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.X.3    Thompson, J.A.4    Beckman, J.S.5
  • 8
    • 0034102513 scopus 로고    scopus 로고
    • The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: Implications for amytrophic lateral sclerosis
    • T.J. Lyons, A. Nersissian, H. Huang, H. Yeom, C.R. Nishida, and J.A. Graden The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amytrophic lateral sclerosis J. Biol. Inorg. Chem. 5 2000 189 203
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 189-203
    • Lyons, T.J.1    Nersissian, A.2    Huang, H.3    Yeom, H.4    Nishida, C.R.5    Graden, J.A.6
  • 9
    • 0037168643 scopus 로고    scopus 로고
    • Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state
    • M.J. Lindberg, L. Tibell, and M. Oliveberg Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state Proc. Natl Acad. Sci. USA 99 2002 16607 16612
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16607-16612
    • Lindberg, M.J.1    Tibell, L.2    Oliveberg, M.3
  • 10
    • 0037013264 scopus 로고    scopus 로고
    • Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • L.J. Hayward, J.A. Rodriguez, J.W. Kim, A. Tiwari, J.J. Goto, and D.E. Cabelli Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis J. Biol. Chem. 277 2002 15923 15931
    • (2002) J. Biol. Chem. , vol.277 , pp. 15923-15931
    • Hayward, L.J.1    Rodriguez, J.A.2    Kim, J.W.3    Tiwari, A.4    Goto, J.J.5    Cabelli, D.E.6
  • 11
    • 0037013224 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper-zinc superoxide dismutase
    • J.A. Roderiguez, J.S. Valentine, D.K. Eggers, J.A. Roe, A. Tiwara, and R.H.J. Brown Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper-zinc superoxide dismutase J. Biol. Chem. 277 2002 15932 15937
    • (2002) J. Biol. Chem. , vol.277 , pp. 15932-15937
    • Roderiguez, J.A.1    Valentine, J.S.2    Eggers, D.K.3    Roe, J.A.4    Tiwara, A.5    Brown, R.H.J.6
  • 12
    • 23844471242 scopus 로고    scopus 로고
    • Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis
    • A. Tiwari, Z. Xu, and L.J. Hayward Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis J. Biol. Chem. 280 2005 29771 29779
    • (2005) J. Biol. Chem. , vol.280 , pp. 29771-29779
    • Tiwari, A.1    Xu, Z.2    Hayward, L.J.3
  • 13
    • 0037795635 scopus 로고    scopus 로고
    • Cu Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro
    • P.B. Stathopulos, J.A.O. Rumfeldt, G.A. Scholz, R.A. Irani, H.E. Frey, and R.A. Hallewell Cu Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro Proc. Natl Acad. Sci. USA 100 2003 7021 7026
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 7021-7026
    • Stathopulos, P.B.1    Rumfeldt, J.A.O.2    Scholz, G.A.3    Irani, R.A.4    Frey, H.E.5    Hallewell, R.A.6
  • 14
    • 9144261759 scopus 로고    scopus 로고
    • The unusually stable quaternary structure of human Cu,Zn sunperxide dismutase 1 is controlled by both metal occupancy and disulfide status
    • F. Arnesano, L. Banci, I. Bertini, M. Martinelli, Y. Furukawa, and T.V. O'Halloran The unusually stable quaternary structure of human Cu,Zn sunperxide dismutase 1 is controlled by both metal occupancy and disulfide status J. Biol. Chem. 279 2004 47998 48003
    • (2004) J. Biol. Chem. , vol.279 , pp. 47998-48003
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Martinelli, M.4    Furukawa, Y.5    O'Halloran, T.V.6
  • 15
    • 11144256229 scopus 로고    scopus 로고
    • Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: Implications for ALS
    • S.M. Lynch, S.A. Boswell, and W. Colon Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS Biochemistry 43 2004 16525 16531
    • (2004) Biochemistry , vol.43 , pp. 16525-16531
    • Lynch, S.M.1    Boswell, S.A.2    Colon, W.3
  • 16
    • 11144227941 scopus 로고    scopus 로고
    • Disassociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability
    • P.A. Doucette, L.J. Whitson, X. Cao, V. Schirf, B. Demeler, and J.S. Valentine Disassociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability J. Biol. Chem. 279 2004 54558 54566
    • (2004) J. Biol. Chem. , vol.279 , pp. 54558-54566
    • Doucette, P.A.1    Whitson, L.J.2    Cao, X.3    Schirf, V.4    Demeler, B.5    Valentine, J.S.6
  • 17
  • 18
  • 19
    • 0037427449 scopus 로고    scopus 로고
    • The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
    • R.W. Strange, S. Antonyuk, M.A. Hough, P.A. Doucette, J.A. Rodriguez, and P.J. Hart The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis J. Mol. Biol. 328 2003 877 891
    • (2003) J. Mol. Biol. , vol.328 , pp. 877-891
    • Strange, R.W.1    Antonyuk, S.2    Hough, M.A.3    Doucette, P.A.4    Rodriguez, J.A.5    Hart, P.J.6
  • 20
    • 0042736853 scopus 로고    scopus 로고
    • ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization
    • M. DiDonato, L. Craig, M.E. Huff, M.M. Thayer, R.M.F. Cardoso, and C.J. Kassmann ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization J. Mol. Biol. 332 2003 601 615
    • (2003) J. Mol. Biol. , vol.332 , pp. 601-615
    • Didonato, M.1    Craig, L.2    Huff, M.E.3    Thayer, M.M.4    Cardoso, R.M.F.5    Kassmann, C.J.6
  • 22
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton Procheck - a program to check the stereochemical quality of protein structures J. Appl. Crystallog. 25 1993 283 291
    • (1993) J. Appl. Crystallog. , vol.25 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 0034055545 scopus 로고    scopus 로고
    • Structural changes in a cryo-cooled protein crystal owing to radiation damage
    • W.P. Burmeister Structural changes in a cryo-cooled protein crystal owing to radiation damage Acta Crystallog. sect. D 56 2000 328 341
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 328-341
    • Burmeister, W.P.1
  • 24
    • 0042131831 scopus 로고    scopus 로고
    • Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 Å
    • M.A. Hough, and S.S. Hasnain Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 Å Structure 11 2003 937 946
    • (2003) Structure , vol.11 , pp. 937-946
    • Hough, M.A.1    Hasnain, S.S.2
  • 25
    • 0034711440 scopus 로고    scopus 로고
    • Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: The importance of mobility in the Glu119-Leu142 loop region for catalytic function
    • M.A. Hough, R.W. Strange, and S.S. Hasnain Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function J. Mol. Biol. 304 2000 231 241
    • (2000) J. Mol. Biol. , vol.304 , pp. 231-241
    • Hough, M.A.1    Strange, R.W.2    Hasnain, S.S.3
  • 26
    • 0033515433 scopus 로고    scopus 로고
    • Crystallographic Structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: Functionally important three and five coordinate copper sites captured in the same crystal
    • M. Hough, and S.S. Hasnain Crystallographic Structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal J. Mol. Biol. 287 1999 579 592
    • (1999) J. Mol. Biol. , vol.287 , pp. 579-592
    • Hough, M.1    Hasnain, S.S.2
  • 27
    • 0037458564 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction
    • A. Tiwari, and L.J. Hayward Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction J. Biol. Chem. 278 2003 5984 5992
    • (2003) J. Biol. Chem. , vol.278 , pp. 5984-5992
    • Tiwari, A.1    Hayward, L.J.2
  • 28
    • 23844471242 scopus 로고    scopus 로고
    • Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-Superoxide dismutase in familial amyotrophic lateral sclerosis
    • A. Tiwari, Z. Xu, and L.J. Hayward Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-Superoxide dismutase in familial amyotrophic lateral sclerosis J. Biol. Chem. 280 2005 29771 29779
    • (2005) J. Biol. Chem. , vol.280 , pp. 29771-29779
    • Tiwari, A.1    Xu, Z.2    Hayward, L.J.3
  • 29
    • 11144357460 scopus 로고    scopus 로고
    • Destabilisation of the dimer interface in SOD1 may result in disease causing properties: Structures of motor neuron disease mutants A4V and I113T
    • M.A. Hough, J.G. Grossman, S.V. Antonyuk, R.W. Strange, P.A. Doucette, and J. Roderiguez Destabilisation of the dimer interface in SOD1 may result in disease causing properties: structures of motor neuron disease mutants A4V and I113T Proc. Natl Acad. Sci. USA 101 2004 5976 5981
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 5976-5981
    • Hough, M.A.1    Grossman, J.G.2    Antonyuk, S.V.3    Strange, R.W.4    Doucette, P.A.5    Roderiguez, J.6
  • 30
    • 1942501776 scopus 로고    scopus 로고
    • A possible theraputic target for Lou Gehrig's disease
    • S.S. Ray, and P.T. Lansbury A possible theraputic target for Lou Gehrig's disease Proc. Natl Acad. Sci. USA 101 2004 5701 5702
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 5701-5702
    • Ray, S.S.1    Lansbury, P.T.2
  • 31
    • 2442624720 scopus 로고    scopus 로고
    • Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis
    • R. Rakhit, J.P. Crow, J.R. Lepock, L.H. Kondejewski, N.R. Cashman, and A. Chakrabartty Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis J. Biol. Chem. 279 2004 15499 15504
    • (2004) J. Biol. Chem. , vol.279 , pp. 15499-15504
    • Rakhit, R.1    Crow, J.P.2    Lepock, J.R.3    Kondejewski, L.H.4    Cashman, N.R.5    Chakrabartty, A.6
  • 32
    • 0033977325 scopus 로고    scopus 로고
    • Loss of in vitro metal in mutant copper-zinc superoxide dismutase associated with familial amyotrophic lateral sclerosis
    • J.J. Goto, H. Zhu, R.J. Sanchez, A.M. Nersissian, E.B. Gralla, and J.S. Valentine Loss of in vitro metal in mutant copper-zinc superoxide dismutase associated with familial amyotrophic lateral sclerosis J. Biol. Chem. 275 2000 1007 1014
    • (2000) J. Biol. Chem. , vol.275 , pp. 1007-1014
    • Goto, J.J.1    Zhu, H.2    Sanchez, R.J.3    Nersissian, A.M.4    Gralla, E.B.5    Valentine, J.S.6
  • 34
    • 0032568546 scopus 로고    scopus 로고
    • Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants
    • L.B. Corson, J. Strain, V.C. Culotta, and D.W. Cleveland Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants Proc. Natl Acad. Sci. USA 95 1998 6361 6366
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6361-6366
    • Corson, L.B.1    Strain, J.2    Culotta, V.C.3    Cleveland, D.W.4
  • 35
    • 0033601223 scopus 로고    scopus 로고
    • A gain of superoxide dismutase (SOD) activity obtained with CCS, the copper metallochaperone for SOD1
    • P.J. Schmidt, M. Ramos-Gomez, and V.C. Culotta A gain of superoxide dismutase (SOD) activity obtained with CCS, the copper metallochaperone for SOD1 J. Biol. Chem. 274 1999 36952 36956
    • (1999) J. Biol. Chem. , vol.274 , pp. 36952-36956
    • Schmidt, P.J.1    Ramos-Gomez, M.2    Culotta, V.C.3
  • 36
    • 0032508609 scopus 로고    scopus 로고
    • The copper chaperone CCS directly interacts with copper/Zinc superoxide dismutase
    • R.L. Casareno, D. Waggoner, and J.D. Gitlin The copper chaperone CCS directly interacts with copper/Zinc superoxide dismutase J. Biol. Chem. 273 1998 23625 23628
    • (1998) J. Biol. Chem. , vol.273 , pp. 23625-23628
    • Casareno, R.L.1    Waggoner, D.2    Gitlin, J.D.3
  • 37
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • T.V. O'Halloran, and V.C. Culotta Metallochaperones, an intracellular shuttle service for metal ions J. Biol. Chem. 275 2000 25057 25060
    • (2000) J. Biol. Chem. , vol.275 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 38
    • 0035914375 scopus 로고    scopus 로고
    • Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase
    • A.S. Torres, V. Petri, T.D. Rae, and T.V. O'Halloran Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase J. Biol. Chem. 276 2001 38410 38416
    • (2001) J. Biol. Chem. , vol.276 , pp. 38410-38416
    • Torres, A.S.1    Petri, V.2    Rae, T.D.3    O'Halloran, T.V.4
  • 39
    • 23844522625 scopus 로고    scopus 로고
    • A high throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler
    • M. Cianci, S. Antonyuk, N. Bliss, S.G. Buffey, K.C. Cheung, and J.A. Clarke A high throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler J. Synchr. Radiat. 12 2005 442 452
    • (2005) J. Synchr. Radiat. , vol.12 , pp. 442-452
    • Cianci, M.1    Antonyuk, S.2    Bliss, N.3    Buffey, S.G.4    Cheung, K.C.5    Clarke, J.A.6
  • 40
    • 0033464412 scopus 로고    scopus 로고
    • A low profile monolithic multi-element Ge X-ray detector for fluorescence applications
    • G. Derbyshire, K.C. Cheung, P. Sangsingkeow, and S.S. Hasnain A low profile monolithic multi-element Ge X-ray detector for fluorescence applications J. Synchr. Radiat. 6 1999 62 63
    • (1999) J. Synchr. Radiat. , vol.6 , pp. 62-63
    • Derbyshire, G.1    Cheung, K.C.2    Sangsingkeow, P.3    Hasnain, S.S.4
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • A.A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J. Appl. Crystallog. 30 1997 1022 1025
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1022-1025
    • Vagin, A.A.1    Teplyakov, A.2
  • 43
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 47
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model building tools for molecular graphics
    • P. Emsley, and K. Cowtan Coot: model building tools for molecular graphics Acta Crystallog. sect. B 60 2004 2126 2132
    • (2004) Acta Crystallog. Sect. B , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.