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Crystal structure of yeast Sco1

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Abstract

The Sco family of proteins are involved in the assembly of the dinuclear CuA site in cytochrome c oxidase (COX), the terminal enzyme in aerobic respiration. These proteins, which are found in both eukaryotes and prokaryotes, are characterized by a conserved CXXXC sequence motif that binds copper ions and that has also been proposed to perform a thiol:disulfide oxidoreductase function. The crystal structures of Saccharomyces cerevisiae apo Sco1 (apo-ySco1) and Sco1 in the presence of copper ions (Cu–ySco1) were determined to 1.8- and 2.3-Å resolutions, respectively. Yeast Sco1 exhibits a thioredoxin-like fold, similar to that observed for human Sco1 and a homolog from Bacillus subtilis. The Cu–ySco1 structure, obtained by soaking apo-ySco1 crystals in copper ions, reveals an unexpected copper-binding site involving Cys181 and Cys216, cysteine residues present in ySco1 but not in other homologs. The conserved CXXXC cysteines, Cys148 and Cys152, can undergo redox chemistry in the crystal. An essential histidine residue, His239, is located on a highly flexible loop, denoted the Sco loop, and can adopt positions proximal to both pairs of cysteines. Interactions between ySco1 and its partner proteins yeast Cox17 and yeast COX2 are likely to occur via complementary electrostatic surfaces. This high-resolution model of a eukaryotic Sco protein provides new insight into Sco copper binding and function.

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Abbreviations

apo-ySco1:

Apo form of ySco1 truncate

BsSco:

Soluble truncate of Bacillus subtilis Sco

COX:

Cytochrome c oxidase

COX1:

Subunit I of cytochrome c oxidase

COX2:

Subunit II of cytochrome c oxidase

COX3:

Subunit III of cytochrome c oxidase

Cu–ySco1:

Copper(I)-soaked form of ySco1 truncate

hSco1:

Soluble truncate of human Sco1

hSco2:

Soluble truncate of human Sco2

IM:

Mitochondrial inner membrane

IMS:

Mitochondrial intermembrane space

rmsd:

Root mean square deviation

TCEP:

Tris(2-carboxylethyl)phosphine

Tris:

Tris(hydroxymethyl)aminomethane

yCox17:

Saccharomyces cerevisiae Cox17

ySco1:

Saccharomyces cerevisiae Sco1 soluble truncate lacking the N-terminal 95 residues

References

  1. Taanman J-W, Capaldi RA (1992) J Biol Chem 267:22481–22485

    PubMed  CAS  Google Scholar 

  2. Carr HS, Winge DR (2003) Acc Chem Res 36:309–316

    Article  PubMed  CAS  Google Scholar 

  3. Ferguson-Miller S, Babcock GT (1996) Chem Rev 96:2889–2908

    Article  PubMed  CAS  Google Scholar 

  4. Tzagoloff A, Dieckmann CL (1990) Microbiol Rev 54:211–225

    PubMed  CAS  Google Scholar 

  5. Glerum DM, Shtanko A, Tzagoloff A (1996) J Biol Chem 271:14504–14509

    Article  PubMed  CAS  Google Scholar 

  6. Punter FA, Glerum DM (2003) J Biol Chem 278:30875–30880

    Article  PubMed  CAS  Google Scholar 

  7. Glerum DM, Shtanko A, Tzagoloff A (1996) J Biol Chem 271:20531–20535

    Article  PubMed  CAS  Google Scholar 

  8. Dickinson EK, Adams DL, Schon EA, Glerum DM (2000) J Biol Chem 275:26780–26875

    Article  PubMed  CAS  Google Scholar 

  9. Heaton D, Nittis T, Srinivasan C, Winge DR (2000) J Biol Chem 275:37582–37587

    Article  PubMed  CAS  Google Scholar 

  10. Beers J, Glerum DM, Tzagoloff A (1997) J Biol Chem 272:33191–33196

    Article  PubMed  CAS  Google Scholar 

  11. Maxfield AB, Heaton DN, Winge DR (2004) J Biol Chem 279:5072–5080

    Article  PubMed  CAS  Google Scholar 

  12. Cobine PA, Ojeda LD, Rigby KM, Winge DR (2004) J Biol Chem 279:14447–14455

    Article  PubMed  CAS  Google Scholar 

  13. Horng Y-C, Cobine PA, Maxfield AB, Carr HS, Winge DR (2004) J Biol Chem 279:35334–35340

    Article  PubMed  CAS  Google Scholar 

  14. Buchwald P, Krummeck G, Rodel G (1991) Mol Gen Genet 229:413–420

    Article  PubMed  CAS  Google Scholar 

  15. Rentzsch A, Krummeck-Weiss G, Hofer A, Bartuschka A, Ostermann K, Rödel G (1999) Curr Genet 35:103–108

    Article  PubMed  CAS  Google Scholar 

  16. Mattatall NR, Jazairi J, Hill BC (2000) J Biol Chem 275:28802–28809

    Article  PubMed  CAS  Google Scholar 

  17. Chinenov YV (2000) J Mol Med 78:239–242

    Article  PubMed  CAS  Google Scholar 

  18. Arnesano F, Banci L, Bertini I, Martinelli M (2005) J Proteome Res 4:63–70

    Article  PubMed  CAS  Google Scholar 

  19. Nittis T, George GN, Winge DR (2001) J Biol Chem 276:42520–42526

    Article  PubMed  CAS  Google Scholar 

  20. Beers J, Glerum DM, Tzagoloff A (2002) J Biol Chem 277:22185–22190

    Article  PubMed  CAS  Google Scholar 

  21. Horng Y-C, Leary SC, Cobine PA, Young FBJ, George GN, Shoubridge EA, Winge DR (2005) J Biol Chem 280:34113–34122

    Article  PubMed  CAS  Google Scholar 

  22. Lode A, Kuschel M, Paret C, Rödel G (2000) FEBS Lett 485:19–24

    Article  PubMed  CAS  Google Scholar 

  23. Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S (2003) Structure 11:1431–1443

    Article  PubMed  CAS  Google Scholar 

  24. Ye Q, Imriskova-Sosova I, Hill BC, Jia Z (2005) Biochemistry 44:2934–2942

    Article  PubMed  CAS  Google Scholar 

  25. Williams JC, Sue C, Banting GS, Yang H, Glerum DM, Hendrickson WA, Schon EA (2005) J Biol Chem 280:15202–15211

    Article  PubMed  CAS  Google Scholar 

  26. Powell HR (1999) Acta Crystallogr Sect D 55:1690–1695

    Article  CAS  Google Scholar 

  27. Kabsch W (1993) J Appl Crystallogr 26:795–800

    Article  CAS  Google Scholar 

  28. Collaborative Computational Project Number 4 (1994) Acta Crystallogr Sect D 50:760–763

    Google Scholar 

  29. Storoni LC, McCoy AJ, Read RJ (2004) Acta Crystallogr Sect D 60:432–438

    Article  Google Scholar 

  30. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang J-S, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL (1998) Acta Crystallogr Sect D 54:905–921

    Article  Google Scholar 

  31. McRee DE (1999) J Struct Biol 125:156–165

    Article  PubMed  CAS  Google Scholar 

  32. Laskowski RA (1993) J Appl Crystallogr 26:283–291

    Article  CAS  Google Scholar 

  33. Delano WL (2002) The PyMOL molecular graphics system. DeLano Scientific, San Carlos, CA

    Google Scholar 

  34. Kleywegt GJ, Jones TA (1994) In: Bailey S, Hubbard R, Waller D (eds) From first map to final model. SERC Daresbury Laboratory, Warrington, pp 59–66

  35. Guex N, Peitsch MC (1997) Electrophoresis 18:2714–2723

    Article  PubMed  CAS  Google Scholar 

  36. Martin JL (1995) Structure 3:245–250

    Article  PubMed  CAS  Google Scholar 

  37. Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE (1998) Nat Struct Biol 5:400–406

    Article  PubMed  CAS  Google Scholar 

  38. Holm L, Sander C (1996) Science 273:595–602

    Article  PubMed  CAS  Google Scholar 

  39. Crow A, Acheson RM, LeBrun NE, Oubrie A (2004) J Biol Chem 279:23654–23660

    Article  PubMed  CAS  Google Scholar 

  40. Cavallini D, De Marco C, Duprè S, Rotilio G (1969) Arch Biochem Biophys 130:354–361

    Article  PubMed  CAS  Google Scholar 

  41. Hiniker A, Collet J-F, Bardwell JCA (2005) J Biol Chem 280:33785–33791

    Article  Google Scholar 

  42. Rosenzweig AC (2001) Acc Chem Res 34:119–128

    Article  PubMed  CAS  Google Scholar 

  43. Mora-García S, Rodríguez-Suárez R, Wolosiuk RA (1998) J Biol Chem 273:16273–16280

    Article  PubMed  Google Scholar 

  44. Dolinsky TJ, Nielsen JE, McCammon JA, Baker NA (2004) Nucleic Acids Res 32:W665–W667

    Article  PubMed  CAS  Google Scholar 

  45. Baker NA, Sept D, Joseph S, Holst MJ, McCammon JA (2001) Proc Natl Acad Sci USA 98:10037–10041

    Article  PubMed  CAS  Google Scholar 

  46. Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC (2004) J Biol Chem 279:53584–53592

    Article  PubMed  CAS  Google Scholar 

  47. Arnesano F, Balatri E, Banci L, Bertini I, Winge DR (2005) Structure 13:713–722

    Article  PubMed  CAS  Google Scholar 

  48. Jaksch M, Paret C, Stucka R, Horn N, Muller-Hocker J, Horvath R, Trepesch N, Stecker G, Freisinger P, Thirion C, Muller J, Lunkwitz R, Rodel G, Shoubridge EA, Lochmuller H (2001) Hum Mol Genet 10:3025–3035

    Article  PubMed  CAS  Google Scholar 

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Acknowledgements

This work was supported by NIH grant GM58518. We thank the staff at the APS DND-CAT beamline for assistance with data collection.

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Authors and Affiliations

  1. Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL, 60208, USA

    Carnie Abajian & Amy C. Rosenzweig

  2. Department of Chemistry, Northwestern University, Evanston, IL, 60208, USA

    Carnie Abajian & Amy C. Rosenzweig

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  1. Carnie Abajian
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  2. Amy C. Rosenzweig
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Correspondence to Amy C. Rosenzweig.

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Abajian, C., Rosenzweig, A.C. Crystal structure of yeast Sco1. J Biol Inorg Chem 11, 459–466 (2006). https://doi.org/10.1007/s00775-006-0096-7

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  • DOI: https://doi.org/10.1007/s00775-006-0096-7

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