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Structure of ribonucleotide reductase protein R1

Nature volume 370, pages 533–539 (1994)Cite this article

Abstract

Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribo-nucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteines. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded α/β-barrel, and two others at the carboxyl end in a flexible arm. The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction.

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References

  1. Elledge, S. J., Zhou, Z. & Allen, J. B. Trends biochem. Sci. 17, 119–123 (1992).

    Article  CAS  Google Scholar 

  2. Tuggle, C. K. & Fuchs, J. A. J. Bact. 172, 1711–1718 (1990).

    Article  CAS  Google Scholar 

  3. Björklund, S., Skog, S., Tribukait, B. & Thelander, L. Biochemistry 29, 5452–5458 (1990).

    Article  Google Scholar 

  4. Reichard, P. Science 260, 1773–1777 (1993).

    Article  ADS  CAS  Google Scholar 

  5. Reichard, P. & Ehrenberg, A. Science 221, 514–519 (1983).

    Article  ADS  CAS  Google Scholar 

  6. Nordlund, P., Sjöberg, B.-M. & Eklund, H. Nature 345, 593–598 (1990).

    Article  ADS  CAS  Google Scholar 

  7. Nordlund, P. & Eklund, H. J. molec. Biol. 232, 123–164 (1993).

    Article  CAS  Google Scholar 

  8. Thelander, L., Larsson, B., Hobbs, J. & Eckstein, F. J. biol. Chem. 251, 1398–1405 (1976).

    CAS  PubMed  Google Scholar 

  9. Mao, S. S. et al. Biochemistry 31, 9733–9743 (1992).

    Article  CAS  Google Scholar 

  10. Mao, S. S. et al. Biochemistry 31, 9744–9751 (1992).

    Article  CAS  Google Scholar 

  11. Mao, S. S., Yu, G. X., Chalfoun, D. & Stubbe, J. Biochemistry 31, 9752–9759 (1992).

    Article  CAS  Google Scholar 

  12. Holmgren, A. J. biol. Chem. 264, 13463–13460 (1989).

    Google Scholar 

  13. Moss, N. et al. J. med. Chem. 36, 3005–3009 (1993).

    Article  CAS  Google Scholar 

  14. Cohen, E. A., Gaudreau, P., Brazeau, P. & Langlier, Y. Nature 321, 441–443 (1986).

    Article  ADS  CAS  Google Scholar 

  15. Dutia, B. M., Frame, M. C., Subak-Sharpe, J. H., Clark, W. N. & Marsden, H. S. Nature 321, 439–441 (1986).

    Article  ADS  CAS  Google Scholar 

  16. Climent, I., Sjöberg, B.-M. & Huang, C. Y. Biochemistry 30, 5164–5171 (1991).

    Article  CAS  Google Scholar 

  17. Uhlin, U., Uhlin, T. & Eklund, H. FEBS Lett. 336, 148–152 (1993).

    Article  CAS  Google Scholar 

  18. Zhang, K. Y. J. & Main, P. Acta crystallogr. A46, 377–381 (1990).

    Article  CAS  Google Scholar 

  19. Jones, T. A. in Molecular Replacement (ed. Dodson, E. J.) 91–105 (SERC, Daresbury, UK, 1992).

    Google Scholar 

  20. Farber, G. K. & Petsko, G. A. Trends biochem. Sci. 15, 228–234 (1990).

    Article  CAS  Google Scholar 

  21. Brändén, C.-I. Curr. Opin. struct. Biol. 1, 978–983 (1991).

    Article  Google Scholar 

  22. Åberg, A. et al. J. biol. Chem. 264, 12249–12252 (1989).

    PubMed  Google Scholar 

  23. Åberg, A. thesis, Univ. Stockholm (1993).

  24. Lin, A.-N.I., Ashley, G. W. & Stubbe, J. Biochemistry 26, 6905–6909 (1987).

    Article  CAS  Google Scholar 

  25. Mao, S. S., Jokuston, M. I., Bollinger, J.-M. & Stubbe, J. Proc. natn. Acad. Sci. U.S.A. 86, 1485–1489 (1989).

    Article  ADS  CAS  Google Scholar 

  26. Karlsson, M., Sahlin, M. & Sjöberg, B.-M. J. biol. Chem. 267, 12622–12626 (1992).

    CAS  PubMed  Google Scholar 

  27. Wilmanns, M., Hyde, C. C., Davies, D. R., Kirschner, K. & Jansonius, J. N. Biochemistry 30, 9161–9169 (1991).

    Article  CAS  Google Scholar 

  28. Booker, S. & Stubbe, J. Proc. natn. Acad. Sci. U.S.A. 90, 8352–8356 (1993).

    Article  ADS  CAS  Google Scholar 

  29. Booker, S., Broderick, J. & Stubbe, J. Biochem. Soc. Trans. 21, 727–730 (1993).

    Article  CAS  Google Scholar 

  30. Climent, I., Sjöberg, B.-M. & Huang, C. Y. Biochemistry 31, 4801–4807 (1992).

    Article  CAS  Google Scholar 

  31. Lycksell, P.-O., Ingemarson, R., Davis, R., Gräslund, A. & Thelander, L. Biochemistry 33, 2838–2842 (1994).

    Article  CAS  Google Scholar 

  32. Schulz, G. E., Schirmer, R. H., Sachsenheimer, W. & Pai, E. F. Nature 273, 120–124 (1978).

    Article  ADS  CAS  Google Scholar 

  33. Prongay, A. J. & Williams, C. H. Jr J. biol. Chem. 265, 18968–18975 (1990).

    CAS  PubMed  Google Scholar 

  34. Eriksson, S., Sjöberg, B.-M., Jörnvall, H. & Carlquist, M. J. biol. Chem. 261, 1878–1882 (1986).

    CAS  PubMed  Google Scholar 

  35. Blum, M., Metcalf, P., Harrison, S. C. & Wiley, D. C. J. appl. Crystallogr. 20, 235–242 (1987).

    Article  CAS  Google Scholar 

  36. Nyborg, J. & Wonacott, A. J. in The Rotation Method in Crystallography 139–152 (North Holland, Amsterdam, 1977).

    Google Scholar 

  37. Otwinowski, Z. Denzo Manual (Yale University, New Haven, 1991).

    Google Scholar 

  38. Knight, S. thesis, Swedish Univ. Agricultural Sciences (1989).

  39. Terwillinger, T. C. & Eisenberg, D. Acta crystallogr. A39, 813–817 (1983).

    Article  Google Scholar 

  40. Otwinowski, Z. MLPHARE, CCP4 Proc. 80-88 (Daresbury Laboratories, Warrington, UK, 1991).

  41. Wang, B. C. Meth. Enzym. 115, 90–112 (1985).

    Article  CAS  Google Scholar 

  42. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Acta crystallogr. 47, 110–119 (1991).

    Article  Google Scholar 

  43. Jones, T. A. & Thirup, S. EMBO J. 5, 819–822 (1986).

    Article  CAS  Google Scholar 

  44. Bricogne, G. Acta crystallogr. A30, 395–405 (1974).

    Article  ADS  Google Scholar 

  45. Brünger, T. A., Kuriyan, J. & Karplus, M. Science 235, 458–460 (1987).

    Article  ADS  Google Scholar 

  46. Kraulis, P. J. appl. Crystallogr. 24, 946–950 (1991).

    Article  Google Scholar 

  47. Presnell, S. R. & Cohen, F. E. Proc. natn. Acad. Sci. U.S.A. 86, 6592–6596 (1989).

    Article  ADS  CAS  Google Scholar 

Download references

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Authors and Affiliations

  1. Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Box 590, S-751 24, Uppsala, Sweden

    Ulla Uhlin & Hans Eklund

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  1. Ulla Uhlin
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  2. Hans Eklund
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Uhlin, U., Eklund, H. Structure of ribonucleotide reductase protein R1. Nature 370, 533–539 (1994). https://doi.org/10.1038/370533a0

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