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:翻訳 工藤高裕 (PDBj)
超酸化物不均化酵素(PDB:2sod)

我々は酸素なしで生きていくことはできない。各細胞は、呼吸において電子の最終受容体として酸素に依存しており、酸素がない場合に比べてずっと多くのエネルギーを食物から得ることができる。ところが酸素は危険な化合物でもある。超酸化物(過剰に電子を持つ酸素)などの反応性酸素は、呼吸酵素から漏れ出し、細胞をむちゃくちゃに壊してしまう。この超酸化物はDNA変異の原因となり、またアミノ酸などの必須分子を作る酵素を攻撃する。これは重大な問題であり、ある研究によると大腸菌の細胞において呼吸経路を輸送される電子10000個中3個が適切な場所に行かず、超酸化物のところに行ってしまう。この潜在的な危険と戦うため、多くの細胞は超酸化物不均化酵素(SuperOxide Dismutase (SOD)、ここに示したのはPDBエントリー 2sod のもの)を作る。この酵素は超酸化物を無毒化する酵素である。

不均化

超酸化物不均化酵素(SOD)はその名前から想像がつくように、超酸化物を不均化する。不均化とは一つの特殊な型の反応を指す言葉で、同じだが逆方向の反応を2つの分子に起こす。SODは2つの超酸化物分子に作用し、一方から余分な電子をはぎとり、もう一方に与える。その結果、一方は電子が減少して通常の酸素になり、もう一方は過剰な電子を持つ。そして、後者は素早く2つの水素イオンを取り込み水素過酸化物を形成する。もちろん水素過酸化物も危険な化合物ではあるが、各細胞は カタラーゼ酵素 を使って無毒化することだろう。

臨床におけるSOD

SODは最近、筋萎縮性側索硬化症(amyotrophic lateral sclerosis、ALS、ルー・ゲーリッグ病 Lou Gehrig's disease とも呼ばれる)と関係していることで悪名高くなっている。この病気は、脳と背骨の腱にある神経細胞が選択的に死んでいき、数年かけて麻痺が徐々に進行する変性疾患で、多くの場合、不思議なことに人生の終わりの方で原因が分からず発症する。但し、約10分の1は遺伝性で、親から遺伝した変異によって引き起こされる。最近の研究によって、その変異の一つはSOD遺伝子にあることが明らかになった。現在、科学者たちはこの病気におけるSODの役割を研究しており、これが明らかになれば新たな診療と治療につながると期待されている。

重金属

様々な超酸化不均化酵素(左上 銅・亜鉛型 PDB:1sos、左下 マンガン型 PDB:1msd、右上 ニッケル型 PDB:1q0d、右下 鉄型 PDB:3sdp)

全ての生物は、いずれかの型のSODを持っているようだが、その超酸化物の処理方法にはいくつかのパターンがある。上図に示した酵素は、それぞれ異なる金属イオンを利用して電子転移反応を行っている。我々の細胞では3種類のSODが作られている。銅・亜鉛SOD(上図左上、PDBエントリー 1sos )は細胞内をただよってあらゆる超酸化物を一掃してくれる。そしてこれに似たものが、粘着性の尾部で作られ、これがSODを細胞外の構造にくっつける。分かれたマンガンSOD(上図左下、PDBエントリー 1msd )は、我々のミトコンドリアで使われている。細菌は異なる型のSOD酵素を作っており、それには鉄SOD(上図右下、PDBエントリー 3sdp )や、普通みられないニッケルを持つSOD(上図右上、PDBエントリー 1q0d )が含まれる。

構造を見る

銅/亜鉛(Cu/Zn)超酸化物不均化酵素(PDB:2sod)

銅/亜鉛(Cu/Zn)超酸化物不均化酵素(PDBエントリー 2sod )は大変有能な酵素である。研究者は、超酸化物の酵素への衝突10回につき1回が反応することを突き止めた。これは予期していたよりもずっと多いものである、というのも、活性部位は酵素表面のごく一部しか占めていないからである。そこで、我々はほとんどの衝突は表面以外の場所で起こっているのではないかと考えた。ところがこの活性部位の形と性質から、この能力に関するヒントが得られる。活性部位は、漏斗の形をしていて、基部には銅イオンと亜鉛イオン(緑色の球)がある。強く正電荷を帯びた金属イオンは、近くにある正電荷を帯びたアミノ酸(青色の球)に沿って存在し、負電荷を帯びた超酸化物(赤色の球)を漏斗の中で導き入れる役割をしている。

2007/09/26 にPDBで "Superoxide Dismutase" のキーワードで検索した結果リストをこちらのリストに掲載しています。

2007/09/26 キーワード検索による関連PDBエントリー一覧
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PDB ID Title Authors Publication Year Journal Name Volume No First Page Pubmed ID
1ap5 Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34. Guan, Y., Hickey, M.J., Borgstahl, G.E., Hallewell, R.A., Lepock, J.R., O'Connor, D., Hsieh, Y., Nick, H.S., Silverman, D.N., Tainer, J.A. 1998 Biochemistry 37 4722 9537987
1ap6 Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34. Guan, Y., Hickey, M.J., Borgstahl, G.E., Hallewell, R.A., Lepock, J.R., O'Connor, D., Hsieh, Y., Nick, H.S., Silverman, D.N., Tainer, J.A. 1998 Biochemistry 37 4722 9537987
1ar4 X-Ray Structure of the Cambialistic Superoxide Dismutase from Propionibacterium Shermanii Active with Fe or Mn Schmidt, M., Meier, B., Parak, F. 1996 J.Biol.Inorg.Chem. 1 532 n/a
1ar5
1avm The Structure of the Azide Coordinated Superoxide Dismutase of P. Shermanii Investigated by X-Ray Structure Analysis, Exafs, Mossbauer-and Epr Spectroscopy Schmidt, M., Scherk, C., Iakovleva, O., Nolting, H.F., Meier, B., Parak, F. 1998 Inorg.Chimica Acta 275-276 65 n/a
1azv Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis. Hart, P.J., Liu, H., Pellegrini, M., Nersissian, A.M., Gralla, E.B., Valentine, J.S., Eisenberg, D. 1998 Protein Sci. 7 545 9541385
1b06 Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 A resolution. Knapp, S., Kardinahl, S., Hellgren, N., Tibbelin, G., Schafer, G., Ladenstein, R. 1999 J.Mol.Biol. 285 689 9878438
1b4l A structure-based mechanism for copper-zinc superoxide dismutase. Hart, P.J., Balbirnie, M.M., Ogihara, N.L., Nersissian, A.M., Weiss, M.S., Valentine, J.S., Eisenberg, D. 1999 Biochemistry 38 2167 10026301
1b4t
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2jcw
1ba9 Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?. Banci, L., Benedetto, M., Bertini, I., Del Conte, R., Piccioli, M., Viezzoli, M.S. 1998 Biochemistry 37 11780 9718300
1bs3 Manipulating the coordination mumber of the ferric iron within the cambialistic superoxide dismutase of Propionibacterium shermanii by changing the pH-value A crystallographic analysis Schmidt, M. 1999 Eur.J.Biochem. 262 117 10231372
1bsm
1bt8
1bzo Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase. Bordo, D., Matak, D., Djinovic-Carugo, K., Rosano, C., Pesce, A., Bolognesi, M., Stroppolo, M.E., Falconi, M., Battistoni, A., Desideri, A. 1999 J.Mol.Biol. 285 283 9878406
1cb4 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. Hough, M.A., Hasnain, S.S. 1999 J.Mol.Biol. 287 579 10092461
1cbj
1cob Crystal structure solution and refinement of the semisynthetic cobalt-substituted bovine erythrocyte superoxide dismutase at 2.0 A resolution. Djinovic, K., Coda, A., Antolini, L., Pelosi, G., Desideri, A., Falconi, M., Rotilio, G., Bolognesi, M. 1992 J.Mol.Biol. 226 227 1619651
1coj The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: structural basis for thermostability. Lim, J.H., Yu, Y.G., Han, Y.S., Cho, S., Ahn, B.Y., Kim, S.H., Cho, Y. 1997 J.Mol.Biol. 270 259 9236127
1d5n Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase. Borgstahl, G.E., Pokross, M., Chehab, R., Sekher, A., Snell, E.H. 2000 J.Mol.Biol. 296 951 10686094
1do5 Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Lamb, A.L., Wernimont, A.K., Pufahl, R.A., O'Halloran, T.V., Rosenzweig, A.C. 2000 Biochemistry 39 1589 10677207
1do6 Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states. Yeh, A.P., Hu, Y., Jenney Jr., F.E., Adams, M.W., Rees, D.C. 2000 Biochemistry 39 2499 10704199
1dqi
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1dsw The solution structure of a monomeric, reduced form of human copper,zinc superoxide dismutase bearing the same charge as the native protein. Banci, L., Bertini, I., Del Conte, R., Fadin, R., Mangani, S., Viezzoli, M.S. 1999 J.Biol.Inorg.Chem. 4 795 10631612
1dt0 Cloning, sequence and crystallographic structure of recombinant iron superoxide dismutase from Pseudomonas ovalis. Bond, C.J., Huang, J., Hajduk, R., Flick, K.E., Heath, P.J., Stoddard, B.L. 2000 Acta Crystallogr.,Sect.D 56 1359 11053832
1e9o 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. Hough, M.A., Strange, R.W., Hasnain, S.S. 2000 J.Mol.Biol. 304 231 11080458
1e9p
1e9q
1ej8 X-ray crystallographic and analytical ultracentrifugation analyses of truncated and full-length yeast copper chaperones for SOD (LYS7): a dimer-dimer model of LYS7-SOD association and copper delivery. Hall, L.T., Sanchez, R.J., Holloway, S.P., Zhu, H., Stine, J.E., Lyons, T.J., Demeler, B., Schirf, V., Hansen, J.C., Nersissian, A.M., Valentine, J.S., Hart, P.J. 2000 Biochemistry 39 3611 10736160
1em1 Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis. Leveque, V.J., Stroupe, M.E., Lepock, J.R., Cabelli, D.E., Tainer, J.A., Nick, H.S., Silverman, D.N. 2000 Biochemistry 39 7131 10852710
1en4 Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase. Edwards, R.A., Whittaker, M.M., Whittaker, J.W., Baker, E.N., Jameson, G.B. 2001 Biochemistry 40 15 11141052
1en5
1en6
1eqw Functional and crystallographic characterization of Salmonella typhimurium Cu,Zn superoxide dismutase coded by the sodCI virulence gene. Pesce, A., Battistoni, A., Stroppolo, M.E., Polizio, F., Nardini, M., Kroll, J.S., Langford, P.R., O'Neill, P., Sette, M., Desideri, A., Bolognesi, M. 2000 J.Mol.Biol. 302 465 10970746
1eso Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. Pesce, A., Capasso, C., Battistoni, A., Folcarelli, S., Rotilio, G., Desideri, A., Bolognesi, M. 1997 J.Mol.Biol. 274 408 9405149
1f18 n/a n/a n/a n/a n/a n/a n/a
1f1a
1f1d
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1fi2 Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Woo, E.J., Dunwell, J.M., Goodenough, P.W., Marvier, A.C., Pickersgill, R.W. 2000 Nat.Struct.Biol. 7 1036 11062559
1fun Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human Cu,Zn superoxide dismutase. Fisher, C.L., Cabelli, D.E., Hallewell, R.A., Beroza, P., Lo, T.P., Getzoff, E.D., Tainer, J.A. 1997 Proteins 29 103 9294870
1gn2 Engineering of an intersubunit disulfide bridge in the iron-superoxide dismutase of Mycobacterium tuberculosis. Bunting, K.A., Cooper, J.B., Tickle, I.J., Young, D.B. 2002 Arch.Biochem.Biophys. 397 69 11747311
1gn3 Engineering a change in metal-ion specificity of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis-- X-ray structure analysis of site-directed mutants. Bunting, K., Cooper, J.B., Badasso, M.O., Tickle, I.J., Newton, M., Wood, S.P., Zhang, Y., Young, D. 1998 Eur.J.Biochem. 251 795 9490054
1gn4
1gn6 X-ray structure analysis of an engineered Fe-superoxide dismutase Gly-Ala mutant with significantly reduced stability to denaturant. Cooper, J.B., Saward, S., Erskine, P.T., Badasso, M.O., Wood, S.P., Zhang, Y., Young, D. 1996 FEBS Lett. 387 105 8674528
1gv3 The 2.0A resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase. Atzenhofer, W., Regelsberger, G., Jacob, U., Peschek, G., Furtmuller, P., Huber, R., Obinger, C. 2002 J.Mol.Biol. 321 479 12162960
1hl4 The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. Strange, R.W., Antonyuk, S., Hough, M.A., Doucette, P.A., Rodriguez, J.A., Hart, P.J., Hayward, L.J., Valentine, J.S., Hasnain, S.S. 2003 J.Mol.Biol. 328 877 12729761
1hl5
1i08 Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity. Edwards, R.A., Whittaker, M.M., Whittaker, J.W., Baker, E.N., Jameson, G.B. 2001 Biochemistry 40 4622 11294629
1i0h
1ib5 Single mutations at the subunit interface modulate copper reactivity in Photobacterium leiognathi Cu,Zn superoxide dismutase. Stroppolo, M.E., Pesce, A., D'Orazio, M., O'Neill, P., Bordo, D., Rosano, C., Milani, M., Battistoni, A., Bolognesi, M., Desideri, A. 2001 J.Mol.Biol. 308 555 11327787
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1ibd
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1ids X-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions. Cooper, J.B., McIntyre, K., Badasso, M.O., Wood, S.P., Zhang, Y., Garbe, T.R., Young, D. 1995 J.Mol.Biol. 246 531 7877174
1isa Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Lah, M.S., Dixon, M.M., Pattridge, K.A., Stallings, W.C., Fee, J.A., Ludwig, M.L. 1995 Biochemistry 34 1646 7849024
1isb
1isc
1mng
1ix9 Structures at 0.90 A resolution of the oxidised and reduced forms of the Y174F mutant of the manganese superoxide dismutase from Escherichia coli Anderson, B.F., Edwards, R.A., Whittaker, M.M., Whittaker, J.W., Baker, E.N., Jameson, G.B. n/a To be Published n/a n/a n/a
1ixb
1ja8 Kinetic analysis of product inhibition in human manganese superoxide dismutase. Hearn, A.S., Stroupe, M.E., Cabelli, D.E., Lepock, J.R., Tainer, J.A., Nick, H.S., Silverman, D.N. 2001 Biochemistry 40 12051 11580280
1jcv Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase. Ogihara, N.L., Parge, H.E., Hart, P.J., Weiss, M.S., Goto, J.J., Crane, B.R., Tsang, J., Slater, K., Roe, J.A., Valentine, J.S., Eisenberg, D., Tainer, J.A. 1996 Biochemistry 35 2316 8652572
1yso
1jk9 Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Lamb, A.L., Torres, A.S., O'Halloran, T.V., Rosenzweig, A.C. 2001 Nat.Struct.Biol. 8 751 11524675
1jr9 Crystallization and preliminary crystallographic analysis of manganese superoxide dismutase from Bacillus halodenitrificans. Liao, J., Li, M., Liu, M.Y., Chang, T., Le Gall, J., Gui, L.L., Zhang, J.P., Liang, D.C., Chang, W.R. 2002 Biochem.Biophys. Res.Commun. 294 60 12054740
1kkc Comparison of the crystal structures of the human manganese superoxide dismutase and the homologous Aspergillus fumigatus allergen at 2-A resolution. Fluckiger, S., Mittl, P.R., Scapozza, L., Fijten, H., Folkers, G., Grutter, M.G., Blaser, K., Crameri, R. 2002 J.Immunol. 168 1267 11801664
1kmg Structure and dynamics of copper-free SOD: The protein before binding copper. Banci, L., Bertini, I., Cantini, F., D'Onofrio, M., Viezzoli, M.S. 2002 Protein Sci. 11 2479 12237469
1l3n The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization Banci, L., Bertini, I., Cramaro, F., Del Conte, R., Viezzoli, M.S. 2002 Eur.J.Biochem. 269 1905 11952792
1luv Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: insertion of valine C gamma into the substrate access channel Hearn, A.S., Stroupe, M.E., Cabelli, D.E., Ramilo, C.A., Luba, J.P., Tainer, J.A., Nick, H.S., Silverman, D.N. 2003 Biochemistry 42 2781 12627943
1luw
1ma1 Structure and properties of the atypical iron superoxide dismutase from Methanobacterium thermoautotrophicum Adams, J.J., Anderson, B.F., Renault, J.P., Verchere-Beaur, C., Morgenstern-Badarau, I., Jameson, G.B. n/a To be published n/a n/a n/a
1mfm The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited. Ferraroni, M., Rypniewski, W., Wilson, K.S., Viezzoli, M.S., Banci, L., Bertini, I., Mangani, S. 1999 J.Mol.Biol. 288 413 10329151
1mmm Distinct Metal Environment in Fe-Substituted Manganese Superoxide Dismutase Provides a Structural Basis of Metal Specificity Edwards, R.A., Whittaker, M.M., Whittaker, J.W., Jameson, G.B., Baker, E.N. 1998 J.Am.Chem.Soc. 120 9684 n/a
1msd Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction. Wagner, U.G., Pattridge, K.A., Ludwig, M.L., Stallings, W.C., Werber, M.M., Oefner, C., Frolow, F., Sussman, J.L. 1993 Protein Sci. 2 814 8495200
1my6 The 1.6 A resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus. Kerfeld, C.A., Yoshida, S., Tran, K.T., Yeates, T.O., Cascio, D., Bottin, H., Berthomieu, C., Sugiura, M., Boussac, A. 2003 J.Biol.Inorg.Chem. 8 707 12827458
1n0j The Structure of Human Mitochondrial Mn3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles Borgstahl, G.E., Parge, H.E., Hickey, M.J., Beyer Jr., W.F., Hallewell, R.A., Tainer, J.A. 1992 Cell (Cambridge,Mass.) 71 107 1394426
1n0n Catalytic and Structural Effects of Amino-Acid Substitution at His30 in Human Manganese Superoxide Dismutase Borgstahl, G.E.O., Parge, H.E., Hickey, M.J., Beyer Jr., W.F., Hallewell, R.A., Tainer, J.A. n/a to be published n/a n/a n/a
1n18 Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase. Cardoso, R.M.F., Thayer, M.M., DiDonato, M., Lo, T.P., Bruns, C.K., Getzoff, E.D., Tainer, J.A. 2002 J.Mol.Biol. 324 247 12441104
1n19
1nb2 Crystal structure of a nucleoside diphosphate kinase from Bacillus halodenitrificans: coexpression of its activity with a Mn-superoxide dismutase. Chen, C.-J., Liu, M.-Y., Chang, T., Chang, W.-C., Wang, B.-C., Le Gall, J. 2003 J.Struct.Biol. 142 247 12713952
1oaj Active-site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase. Cioni, P., Pesce, A., Morozzo della Rocca, B., Castelli, S., Falconi, M., Parrilli, L., Bolognesi, M., Strambini, G., Desideri, A. 2003 J.Mol.Biol. 326 1351 12595249
1oal
1oez Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Elam, J.S., Taylor, A.B., Strange, R., Antonyuk, S., Doucette, P.A., Rodriguez, J.A., Hasnain, S.S., Hayward, L.J., Valentine, J.S., Yeates, T.O., Hart, P.J. 2003 Nat.Struct.Biol. 10 461 12754496
1ozt Amyloid-like Filaments and Water-filled Nanotubes Formed by SOD1 Mutant Proteins Linked to Familial ALS Elam, J.S., Taylor, A.B., Strange, R., Antonyuk, S., Doucette, P.A., Rodriguez, J.A., Hasnain, S.S., Hayward, L.J., Valentine, J.S., Yeates, T.O., Hart, P.J. 2003 Nat.Struct.Biol. 10 461 12754496
1ozu
1p1v An Alternative Mechanism of Bicarbonate-mediated Peroxidation by Copper-Zinc Superoxide Dismutase: RATES ENHANCED VIA PROPOSED ENZYME-ASSOCIATED PEROXYCARBONATE INTERMEDIATE Elam, J.S., Malek, K., Rodriguez, J.A., Doucette, P.A., Taylor, A.B., Hayward, L.J., Cabelli, D.E., Valentine, J.S., Hart, P.J. 2003 J.Biol.Chem. 278 21032 12649272
1p7g Structure of superoxide dismutase from Pyrobaculum aerophilum presents a challenging case in molecular replacement with multiple molecules, pseudo-symmetry and twinning. Lee, S., Sawaya, M.R., Eisenberg, D. 2003 Acta Crystallogr.,Sect.D 59 2191 14646077
1pl4 Amino acid substitution at the dimeric interface of human manganese superoxide dismutase Hearn, A.S., Fan, L., Lepock, J.R., Luba, J.P., Greenleaf, W.B., Cabelli, D.E., Tainer, J.A., Nick, H.S., Silverman, D.N. 2004 J.Biol.Chem. 279 5861 14638684
1pm9
1ptz ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization DiDonato, M., Craig, L., Huff, M.E., Thayer, M.M., Cardoso, R.M.F., Kassmann, C.J., Lo, T.P., Bruns, C.K., Powers, E.T., Kelly, J.W., Getzoff, E.D., Tainer, J.A. 2003 J.Mol.Biol. 332 601 12963370
1pu0
1pzs Unique Features of the sodC-encoded Superoxide Dismutase from Mycobacterium tuberculosis, a Fully Functional Copper-containing Enzyme Lacking Zinc in the Active Site. Spagnolo, L., Toro, I., D'Orazio, M., O'Neill, P., Pedersen, J.Z., Carugo, O., Rotilio, G., Battistoni, A., Djinovic-Carugo, K. 2004 J.Biol.Chem. 279 33447 15155722
1q0d Crystal structure of nickel-containing superoxide dismutase reveals another type of active site Wuerges, J., Lee, J.-W., Yim, Y.-I., Yim, H.-S., Kang, S.-O., Djinovic Carugo, K. 2004 Proc.Natl.Acad.Sci.USA 101 8569 15173586
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1q0e Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A. Hough, M.A., Hasnain, S.S. 2003 Structure 11 937 12906825
1qnm Probing the active site of human manganese superoxide dismutase: the role of glutamine 143. Hsieh, Y., Guan, Y., Tu, C., Bratt, P.J., Angerhofer, A., Lepock, J.R., Hickey, M.J., Tainer, J.A., Nick, H.S., Silverman, D.N. 1998 Biochemistry 37 4731 9537988
1qnn Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis. Sugio, S., Hiraoka, B.Y., Yamakura, F. 2000 Eur.J.Biochem. 267 3487 10848964
1qup Crystal structure of the copper chaperone for superoxide dismutase. Lamb, A.L., Wernimont, A.K., Pufahl, R.A., Culotta, V.C., O'Halloran, T.V., Rosenzweig, A.C. 1999 Nat.Struct.Biol. 6 724 10426947
1rk7 Solution structure of Apo Cu,Zn Superoxide Dismutase: Role of Metal Ions in Protein Folding Banci, L., Bertini, I., Cramaro, F., Del Conte, R., Viezzoli, M.S. 2003 Biochemistry 42 9543 12911296
1s4i A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. Banci, L., Bertini, I., Calderone, V., Cramaro, F., Del Conte, R., Fantoni, A., Mangani, S., Quattrone, A., Viezzoli, M.S. 2005 Proc.Natl.Acad.Sci.Usa 102 7541 15897454
1u3n
1sda Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase. Smith, C.D., Carson, M., van der Woerd, M., Chen, J., Ischiropoulos, H., Beckman, J.S. 1992 Arch.Biochem.Biophys. 299 350 1444476
1sdy Structure solution and molecular dynamics refinement of the yeast Cu,Zn enzyme superoxide dismutase. Djinovic, K., Gatti, G., Coda, A., Antolini, L., Pelosi, G., Desideri, A., Falconi, M., Marmocchi, F., Rolilio, G., Bolognesi, M. 1991 Acta Crystallogr., Sect.B 47 918 1772629
1sos Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Parge, H.E., Hallewell, R.A., Tainer, J.A. 1992 Proc.Natl.Acad.Sci.USA 89 6109 1463506
1spd Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Deng, H.X., Hentati, A., Tainer, J.A., Iqbal, Z., Cayabyab, A., Hung, W.Y., Getzoff, E.D., Hu, P., Herzfeldt, B., Roos, R.P., al., et 1993 Science 261 1047 8351519
1srd Three-dimensional structure of Cu,Zn-superoxide dismutase from spinach at 2.0 A resolution. Kitagawa, Y., Tanaka, N., Hata, Y., Kusunoki, M., Lee, G.P., Katsube, Y., Asada, K., Aibara, S., Morita, Y. 1991 J.Biochem.(Tokyo) 109 477 1880134
1sxa Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 A resolution. Rypniewski, W.R., Mangani, S., Bruni, B., Orioli, P.L., Casati, M., Wilson, K.S. 1995 J.Mol.Biol. 251 282 7643403
1sxb
1sxc
1sxn Crystallographic determination of reduced bovine superoxide dismutase at pH 5.0 and of anion binding to its active site. Ferraroni, M., Rypniewski, W.R., Bruni, B., Orioli, P., Mangani, S. 1998 J.Biol.Inorg.Chem. 3 411 n/a
1sxs Crystallographic determination of reduced bovine superoxide dismutase at pH 5.0 and of anion binding to its active site Ferraroni, M., Rypniewski, W.R., Bruni, B., Orioli, P., Mangani, S. 1998 J.Biol.Inorg.Chem. 3 411 n/a
1sxz
1szx Role of hydrogen bonding in the active site of human manganese superoxide dismutase. Greenleaf, W.B., Perry, J.J., Hearn, A.S., Cabelli, D.E., Lepock, J.R., Stroupe, M.E., Tainer, J.A., Nick, H.S., Silverman, D.N. 2004 Biochemistry 43 7038 15170341
1t6i Nickel superoxide dismutase structure and mechanism. Barondeau, D.P., Kassmann, C.J., Bruns, C.K., Tainer, J.A., Getzoff, E.D. 2004 Biochemistry 43 8038 15209499
1t6q
1t6u
1to4 Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni. Cardoso, R.M., Silva, C.H., Ulian de Araujo, A.P., Tanaka, T., Tanaka, M., Garratt, R.C. 2004 Acta Crystallogr.,Sect.D 60 1569 15333927
1to5
1uer Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site Yamakura, F., Sugio, S., Hiraoka, B.Y., Ohmori, D., Yokota, T. 2003 Biochemistry 42 10790 12962504
1ues
1unf The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis. Moran, J.F., Becana, M., Montoya, G. 2005 Protein Sci. 14 387 15659371
1uxl Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. Hough, M.A., Grossmann, J.G., Antonyuk, S.V., Strange, R.W., Doucette, P.A., Rodriguez, J.A., Whitson, L.J., Hart, P.J., Hayward, L.J., Valentine, J.S., Hasnain, S.S. 2004 Proc.Natl.Acad.Sci.Usa 101 5976 15056757
1uxm
1var Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface. Borgstahl, G.E., Parge, H.E., Hickey, M.J., Johnson, M.J., Boissinot, M., Hallewell, R.A., Lepock, J.R., Cabelli, D.E., Tainer, J.A. 1996 Biochemistry 35 4287 8605177
1vew Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-angstrom resolution. Edwards, R.A., Baker, H.M., Whittaker, M.M., Whittaker, J.W., Jameson, G.B., Baker, E.N. 1998 J.Biol.Inorg.Chem. 3 161 n/a
1wb7 The role of Tyr41 and His155 in the functional properties of superoxide dismutase from the archaeon Sulfolobus solfataricus. Gogliettino, M.A., Tanfani, F., Scire, A., Ursby, T., Adinolfi, B.S., Cacciamani, T., De Vendittis, E. 2004 Biochemistry 43 2199 14979716
1wb8 Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: analysis of structure and thermostability. Ursby, T., Adinolfi, B.S., Al-Karadaghi, S., De Vendittis, E., Bocchini, V. 1999 J.Mol.Biol. 286 189 9931259
1xdc Hydrogen bonding in human manganese superoxide dismutase containing 3-fluorotyrosine Ayala, I., Perry, J.J., Szczepanski, J., Tainer, J.A., Vala, M.T., Nick, H.S., Silverman, D.N. 2005 Biophys.J. 89 4171 16150974
1xil
1xre Structures of two superoxide dismutases from Bacillus anthracis reveal a novel active centre. Boucher, I.W., Kalliomaa, A.K., Levdikov, V.M., Blagova, E.V., Fogg, M.J., Brannigan, J.A., Wilson, K.S., Wilkinson, A.J. 2005 Acta Crystallogr.,Sect.F 61 621 16511113
1xuq
1xso Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5 A resolution. Carugo, K.D., Battistoni, A., Carri, M.T., Polticelli, F., Desideri, A., Rotilio, G., Coda, A., Wilson, K.S., Bolognesi, M. 1996 Acta Crystallogr.,Sect.D 52 176 15299740
1xtl From an Inactive Prokaryotic SOD Homologue to an Active Protein through Site-Directed Mutagenesis. Banci, L., Benvenuti, M., Bertini, I., Cabelli, D.E., Calderone, V., Fantoni, A., Mangani, S., Migliardi, M., Viezzoli, M.S. 2005 J.Am.Chem.Soc. 127 13287 16173759
1xtm
1y67 Crystal Structure of Manganese Superoxide Dismutase from Deinococcus radiodurans Chan, S., Tanaka, S., Sawaya, M.R., Perry, L.J. n/a To be Published n/a n/a n/a
1y7n Solution structure of the second PDZ domain of the neuronal adaptor X11alpha and its interaction with the C-terminal peptide of the human copper chaperone for superoxide dismutase Duquesne, A.E., de Ruijter, M., Brouwer, J., Drijfhout, J.W., Nabuurs, S.B., Spronk, C.A.E.M., Vuister, G.W., Ubbink, M., Canters, G.W. 2005 J.Biomol.Nmr 32 209 16132821
1yai Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase. Bourne, Y., Redford, S.M., Steinman, H.M., Lepock, J.R., Tainer, J.A., Getzoff, E.D. 1996 Proc.Natl.Acad.Sci.USA 93 12774 8917495
1z9n X-Ray structure of a Cu-Zn superoxide dismutase from Haemophilus ducreyi with haem bound at the dimer interface Djinovic Carugo, K., Toeroe, I. n/a To be Published n/a n/a n/a
1z9p X-Ray structure of a Cu-Zn superoxide dismutase from Haemophilus ducreyi Djinovic Carugo, K., Toeroe, I., Battistoni, A. n/a To be Published n/a n/a n/a
1za5 The Crucial Importance of Chemistry in the Structure-Function Link: Manipulating Hydrogen Bonding in Iron-Containing Superoxide Dismutase. Yikilmaz, E., Rodgers, D.W., Miller, A.F. 2006 Biochemistry 45 1151 16430211
1zlz Azide Adduct of the Y174F mutant of Manganese superoxide dismutase from Escherichia coli Salvador, J.R., Whittaker, M.M., Whittaker, J.W., Jameson, G.B. n/a To be Published n/a n/a n/a
1zsp Contribution to Structure and Catalysis of Tyrosine 34 in Human Manganese Superoxide Dismutase Hearn, A.S., Perry, J.J., Cabelli, D.E., Tainer, J.A., Nick, H.S., Silverman, D.S. n/a To be Published n/a n/a n/a
1zte
1zuq
2a03 Hypothetical protein from plasmodium berghei Holmes, M.A., Merritt, E.A., Structural Genomics of Pathogenic Protozoa Consortium (SGPP) n/a To be published n/a n/a n/a
2adp Crystal structure of nitrated human manganese superoxide dismutase: mechanism of inactivation. Quint, P., Reutzel, R., Mikulski, R., McKenna, R., Silverman, D.N. 2006 Free Radic.Biol.Med. 40 453 16443160
2adq
2aeo Structural investigation of cisplatin-protein interactions: selective platination of His19 in a cuprozinc superoxide dismutase Calderone, V., Casini, A., Mangani, S., Messori, L., Orioli, P.L. 2006 Angew.Chem.Int.Ed.Engl. 45 1267 16416478
2af2 Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form Banci, L., Bertini, I., Cantini, F., D'Amelio, N., Gaggelli, E. 2006 J.Biol.Chem. 281 2333 16291742
2aps Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface. Forest, K.T., Langford, P.R., Kroll, J.S., Getzoff, E.D. 2000 J.Mol.Biol. 296 145 10656823
2aqm CU/ZN superoxide dismutase from brucella abortus DiDonato, M., Kassmann, C.J., Bruns, C.K., Cabelli, D.E., Cao, Z., Tabatabai, L.B., Kroll, J.S., Getzoff, E.D. n/a To be Published n/a n/a n/a
2aqn CU/ZN superoxide dismutase from neisseria meningitidis DiDonato, M., Kassmann, C.J., Bruns, C.K., Cabelli, D.E., Cao, Z., Tabatabai, L.B., Kroll, J.S., Getzoff, E.D. n/a To be Published n/a n/a n/a
2aqp CU/ZN superoxide dismutase from neisseria meningitidis E73A mutant DiDonato, M., Kassmann, C.J., Bruns, C.K., Cabelli, D.E., Cao, Z., Tabatabai, L.B., Kroll, J.S., Getzoff, E.D. n/a To be Published n/a n/a n/a
2aqq CU/ZN superoxid dismutate from neisseria meningitidis K91E mutant DiDonato, M., Kassmann, C.J., Bruns, C.K., Cabelli, D.E., Cao, Z., Tabatabai, L.B., Kroll, J.S., Getzoff, E.D. n/a To be Published n/a n/a n/a
2aqr CU/ZN superoxide dismutase from neisseria meningitidis K91Q mutant DiDonato, M., Kassmann, C.J., Bruns, C.K., Cabelli, D.E., Cao, Z., Tabatabai, L.B., Kroll, J.S., Getzoff, E.D. n/a To be Published n/a n/a n/a
2aqs CU/ZN superoxide dismutase from neisseria meningitidis K91E, K94E double mutant DiDonato, M., Kassmann, C.J., Bruns, C.K., Cabelli, D.E., Cao, Z., Tabatabai, L.B., Kroll, J.S., Getzoff, E.D. n/a To be Published n/a n/a n/a
2aqt CU/ZN superoxide dismutase from neisseria meningitidis K91Q, K94Q double mutant DiDonato, M., Kassmann, C.J., Bruns, C.K., Cabelli, D.E., Cao, Z., Tabatabai, L.B., Kroll, J.S., Getzoff, E.D. n/a To be Published n/a n/a n/a
2aw9 Crystal structure of manganese superoxide dismutase from Deinococcus radiodurans Tanaka, S., Sawaya, M.R., Chan, S., Perry, L.J. n/a To be Published n/a n/a n/a
2bkb The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase. Yikilmaz, E., Rodgers, D.W., Miller, A.F. 2006 Biochemistry 45 1151 16430211
2bpi The crystal structure of superoxide dismutase from Plasmodium falciparum. Boucher, I.W., Brzozowski, A.M., Brannigan, J.A., Schnick, C., Smith, D.J., Kyes, S.A., Wilkinson, A.J. 2006 Bmc Struct.Biol. 6 20 17020617
2c9s Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. Strange, R.W., Antonyuk, S.V., Hough, M.A., Doucette, P.A., Valentine, J.S., Hasnain, S.S. 2006 J.Mol.Biol. 356 1152 16406071
2c9u
2c9v
2cdy Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms. Dennis, R.J., Micossi, E., McCarthy, J., Moe, E., Gordon, E.J., Kozielski-Stuhrmann, S., Leonard, G.A., McSweeney, S. 2006 Acta Crystallogr.,Sect.F 62 325 16582477
2ce4
2crl The apo form of HMA domain of copper chaperone for superoxide dismutase Nagashima, T., Hayashi, F., Yokoyama, S. n/a To be published n/a n/a n/a
2cw2 Structures of PmSOD1 and PmSOD2, two superoxide dismutases from the protozoan parasite Perkinsus marinus Asojo, O.A., Schott, E.J., Vasta, G.R., Silva, A.M. 2006 Acta Crystallogr.,Sect.F 62 1072 17077482
2cw3
2gbt The Coupling between Disulphide Status, Metallation and Dimer Interface Strength in Cu/Zn Superoxide Dismutase Hornberg, A., Logan, D.T., Marklund, S.L., Oliveberg, M. 2007 J.Mol.Biol. 365 333 17070542
2gbu
2gbv
2gds Interrupting the Hydrogen Bond Network at the Active Site of Human Manganese Superoxide Dismutase Ramilo, C.A., Leveque, V., Guan, Y., Lepock, J.R., Tainer, J.A., Nick, H.S., Silverman, D.N. 1999 J.Biol.Chem. 274 27711 10488113
2goj Systematic structural studies of iron superoxide dismutases from human parasites: a potential target for novel therapeutic agents Navarro, M.V.A.S., Bachega, J.F.R., Bortoleto, R.K., Dive, D., Hoffmann, P., Viscogliosi, E., Araujo, A.P.U., Garratt, R.C. n/a To Be Published n/a n/a n/a
2gpc
2nnx Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability Wang, J., Caruano-Yzermans, A., Rodriguez, A., Scheurmann, J.P., Slunt, H.H., Cao, X., Gitlin, J., Hart, P.J., Borchelt, D.R. 2007 J.Biol.Chem. 282 345 17092942
2nyb How Can a Single Second Sphere Amino Acid Substitution Cause Reduction Midpoint Potential Changes of Hundreds of Millivolts? Yikilmaz, E., Porta, J., Grove, L.E., Vahedi-Faridi, A., Bronshteyn, Y., Brunold, T.C., Borgstahl, G.E., Miller, A.F. 2007 J.Am.Chem.Soc. 129 9927 17628062
2p4k Contribution to structure and catalysis of tyrosine 34 in Human manganese superoxide dismutase Hearn, A.S., Perry, J.J., Cabelli, D.E., Tainer, J.A., Nick, H.S., Silverman, D.S. n/a To be Published n/a n/a n/a
2sod Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. Tainer, J.A., Getzoff, E.D., Beem, K.M., Richardson, J.S., Richardson, D.C. 1982 J.Mol.Biol. 160 181 7175933
2v0a Molecular Dynamics Using Atomic-Resolution Structure Reveal Structural Fluctuations that May Lead to Polymerization of Human Cu-Zn Superoxide Dismutase. Strange, R.W., Yong, C.W., Smith, W., Hasnain, S.S. 2007 Proc.Natl.Acad.Sci.USA 104 10040 17548825
3mds Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 A resolution. Ludwig, M.L., Metzger, A.L., Pattridge, K.A., Stallings, W.C. 1991 J.Mol.Biol. 219 335 2038060
3sdp The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis. Stoddard, B.L., Howell, P.L., Ringe, D., Petsko, G.A. 1990 Biochemistry 29 8885 2271564
3sod Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine. McRee, D.E., Redford, S.M., Getzoff, E.D., Lepock, J.R., Hallewell, R.A., Tainer, J.A. 1990 J.Biol.Chem. 265 14234 2387847

超酸化物不均化酵素についてさらに知りたい方へ

以下の参考文献もご参照ください。

  • P. Pasinelli and R. H. Brown (2006) Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nature Reviews Neuroscience 7
  • J. A. Imlay and I. Fridovich (1991) Assay of metabolic superoxide production in Escherichia coli. Journal of Biological Chemistry 266
  • I. Fridovich (1989) Superoxide dismutases. Journal of Biological Chemistry 264
  • E. D. Getzoff, J. A. Tainer, P. K. Weiner, P. A. Kollman, J. S. Richardson and D. C. Richardson (1983) Electrostatic recognition between superoxide and copper, zinc superoxide dismutase. Nature 306



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