Crystal structures of holo and Cu-deficient Cu/Zn-SOD from the silkworm Bombyx mori and the implications in amyotrophic lateral sclerosis

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 8, 2010, Pages 1999-2004

  Zhang, Nan Nan ^a   He, Yong Xing ^a   Li, Wei Fang ^a   Teng, Yan Bin ^a   Yu, Jiang ^a   Chen, Yuxing ^a   Zhou, Cong Zhao ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

Author keywords

Aggregation; Amyotrophic; Bombyx mori; Cu Zn superoxide dismutase; Fibril; Lateral sclerosis; Protein structure

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; MUSCLE PROTEIN;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; SILKWORM;

AMINO ACID SEQUENCE; AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; BOMBYX; CATALYTIC DOMAIN; COPPER; CRYSTALLOGRAPHY, X-RAY; HOLOENZYMES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SUPEROXIDE DISMUTASE;

BOMBYX MORI;

EID: 77953513699     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22709     Document Type: Article

References (32)

1. Mccord JM, Fridovich I. The utility of superoxide dismutase in studying free radical reactions. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen. J Biol Chem. 1969; 244: 6056-6063.
2. Fridovich I. Superoxide dismutases. Annu Rev Biochem 1975; 44: 147-159.
3. Tainer JA, Getzoff ED, Beem KM, Richardson JS, Richardson DC. Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. J Mol Biol 1982; 160: 181-217.
4. Stroppolo ME, Falconi M, Caccuri AM, Desideri A. Superefficient enzymes. Cell Mol Life Sci 2001; 58: 1451-1460.
5. Brown RH. Superoxide dismutase in familial amyotrophic lateral sclerosis: models for gain of function. Curr Opin Neurobiol 1995; 5: 841-846. (Pubitemid 26042636)
6. Brown RH. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell 1995; 80: 687-692.
7. Deng HX, Hentati A, Tainer JA, Iqbal Z, Cayabyab A, Hung WY, Getzoff ED, Hu P, Herzfeldt B, Roos RP, Warner C, Deng G, Soriano E, Smyth C, Parge HE, Ahmed A, Roses AD, Hallewell RA, Pericak-Vance MA, Siddique T. Amyotrophic lateral sclerosis and structural defects in Cu, Zn superoxide dismutase. Science 1993; 261: 1047-1051.
8. Borchelt DR, Guarnieri M, Wong PC, Lee MK, Slunt HS, Xu ZS, Sisodia SS, Price DL, Cleveland DW. Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function. J Biol. Chem 1995; 270: 3234-3238.
9. Rabizadeh S, Gralla EB, Borchelt DR, Gwinn R, Valentine JS, Sisodia S, Wong P, Lee M, Hahn H, Bredesen DE. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc Natl Acad Sci USA 1995; 92: 3024-3028.
10. Tu PH, Raju P, Robinson KA, Gurney ME, Trojanowski JQ, Lee VM. Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions. Proc Natl Acad Sci USA 1996; 93: 3155-3160. (Pubitemid 26114380)
11. Reaume AG, Elliott JL, Hoffman EK, Kowall NW, Ferrante RJ, Siwek DF, Wilcox HM, Flood DG, Beal MF, Brown RH, Scott RW, Snider WD. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat Genet 1996; 13: 43-47.
12. Furukawa Y, Fu R, Deng HX, Siddique T, O'halloran TV. Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice. Proc Natl Acad Sci USA 2006; 103: 7148-7153.
13. Hart PJ. Pathogenic superoxide dismutase structure, folding, aggregation and turnover. Curr Opin Chem Biol 2006; 10: 131-138.
14. Elam JS, Taylor AB, Strange R, Antonyuk S, Doucette PA, Rodriguez JA, Hasnain SS, Hayward LJ, Valentine JS, Yeates TO, Hart PJ. Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nat Struct Biol 2003; 10: 461-467. (Pubitemid 36637644)
15. Antonyuk S, Elam JS, Hough MA, Strange RW, Doucette PA, Rodriguez JA, Hayward LJ, Valentine JS, Hart PJ, Hasnain SS. Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant his 46arg. Protein Sci 2005; 14: 1201-1213. (Pubitemid 40577800)
16. Didonato M, Craig L, Huff ME, Thayer MM, Cardoso RM, Kassmann CJ, Lo TP, Bruns CK, Powers ET, Kelly JW, Getzoff ED, Tainer JA. ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilizatiou. J Mol Biol 2003; 332: 601-615. (Pubitemid 37075984)
17. Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci USA 2002; 99: 2754-2759.
18. Corpet F. Multiple sequence alignment with hierarchical clustering. Nud Acids Res 1988; 16: 10881-10890.
19. Gouet P, Robert X, Courcelle E. ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins. Nucl Acids Res 2003; 31: 3320-3323. (Pubitemid 37442149)
20. Leslie AGW. Recent changes to the mosflm package for processing film and image plate data. Joint CCP4 1 ESF-EAMCB Newsletter on Protein Crystallography 1992; 26.
21. Evans PR. Data reduction, In: Proceedings of CCP4 Study Weekend, on Data Collection and Processing, Warrington: Daresbury Laboratory; 1993, pp 114-122.
22. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromol Crystallogr 1997; 276: 307-326. (Pubitemid 27085611)
23. Vagin A, Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Crystallogr 1997; 30: 1022-1025. (Pubitemid 127485985)
24. Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr 1997; 53(Part 3): 240-255.
25. Leslie, AGW. The CCP4 suite: programs for protein crystallography. Acta Crystallogr 1994; 50: 760-763.
26. Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta. Crystallogr 2004; 60: 2126-2132. (Pubitemid 41742764)
27. Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WB, Snoeyink J, Richardson JS, Richardson DC. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucl Acids Res 2007; 35: W375-W383.
28. Laskowski RA, Macarthur MW, Moss DS, Thornton JM. Procheck a Program to Check the Stereochemical Quality of Protein Structures. J Appl Crystallogr 1993; 26: 283-291.
29. Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007; 372: 774-797. (Pubitemid 47321791)
30. Delano WL. The PyMOL Molecular Graphics System, San Carlos, CA: DeLano Scientific LLC.
31. Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ. Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. J Biol Chem 2008; 283: 16169-16177.
32. Watson MR, Lagow RD, Xu K, Zhang B, Bonini NM. A drosophila model for amyotrophic lateral sclerosis reveals motor neuron damage by human SOD1, J Biol Chem 2008; 283: 24972-24981.