The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass

Science

Volumn 305, Issue 5681, 2004, Pages 245-248

  Högbom, Martin ^a,d   Stenmark, Pål ^a   Voevodskaya, Nina ^b   McClarty, Grant ^c   Gräslund, Astrid ^b   Nordlund, Pär ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b STOCKHOLM UNIVERSITY   (Sweden)

^c UNIVERSITY OF MANITOBA   (Canada)

^d UPPSALA UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

LIGANDS; RECONSTITUTION;

DNA; ENZYMES; FREE RADICALS; MICROORGANISMS; PARAMAGNETISM;

GENETIC ENGINEERING;

BACTERIAL DNA; DEOXYRIBONUCLEOTIDE; FREE RADICAL; RIBONUCLEOTIDE REDUCTASE; UNSPECIFIC MONOOXYGENASE;

BIOLOGY;

ARTICLE; CHLAMYDIA; CHLAMYDIA TRACHOMATIS; DNA SYNTHESIS; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; CHLAMYDIA TRACHOMATIS; CRYSTALLOGRAPHY, X-RAY; ELECTRON SPIN RESONANCE SPECTROSCOPY; FREE RADICALS; HYDROGEN BONDING; IRON; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXYGEN; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RIBONUCLEOTIDE REDUCTASES; TYROSINE;

BACTERIA (MICROORGANISMS); CHLAMYDIA TRACHOMATIS; RICKETTSIALES;

EID: 3042728737     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1098419     Document Type: Article

References (35)

1. J. W. Moulder, Microbiol. Rev. 55, 143 (1991).
2. R. C. Brunham et al., J. Infect. Dis. 173, 950 (1996).
3. B. M. Sjöberg, Struct. Bonding 88, 139 (1997).
4. H. Eklund, U. Uhlin, M. Farnegardh, D. T. Logan, P. Nordlund, Prog. Biophys. Mol. Biol. 77, 177 (2001).
5. J. Stubbe, D. G. Nocera, C. S. Yee, M. C. Y. Chang, Chem. Rev. 103, 2167 (2003).
6. U. Uhlin, H. Eklund, Nature 370, 533 (1994).
7. P. Nordlund, B.-M. Sjöberg, H. Eklund, Nature 345, 593 (1990).
8. A. Larsson, B. M. Sjoberg, EMBO J. 5, 2037 (1986).
9. M. Högbom et al., Proc. Natl. Acad. Sci. U.S.A. 100, 3209 (2003).
10. A. Jordan, P. Reichard, Annu. Rev. Biochem. 67, 71 (1998).
11. S. Pötsch et al., J. Biol. Chem. 274, 17696 (1999).
12. M. A. Henriksen, B. S. Cooperman, J. S. Salem, J. S. Li, H. Rubin, J. Am. Chem. Soc. 116, 9773 (1994).
13. G. McClarty, G. Tipples, J. Bacteriol. 173, 4922 (1991).
14. G. Tipples, G. McClarty, Mol. Mirobiol. 8, 1105 (1993).
15. C. Roshick, E. R. Iliffe-Lee, G. McClarty, J. Biol. Chem. 275, 38111 (2000).
16. Materials and methods are available as supporting material on Science Online.
17. M. Merkx et al., Angew. Chem. Int. Ed. Engl. 40, 2782 (2001).
18. J. M. Bollinger et al., Science 253, 292 (1991).
19. B. E. Sturgeon et al., J. Am. Chem. Soc. 118, 7551 (1996).
20. D. Yun et al., Biochemistry 41, 981 (2002).
21. J. Baldwin et al., J. Am. Chem. Soc. 122, 1219S (2000).
22. J. M. Bollinger et al., J. Am. Chem. Soc. 116, 8024 (1994).
23. D. Burdi et al., J. Am. Chem. Soc. 120, 12910 (1998).
24. P. J. Riggs-Gelasco et al., J. Am. Chem. Soc. 120, 849 (1998).
25. M. Fontecave, R. Eliasson, P. Reichard, J. Biol. Chem. 262, 12325 (1987).
26. G. Tipples, G. McClarty, J. Bacteriol. 173, 4932 (1991).
27. E. Elleingand et al., Eur. J. Biochem. 258, 485 (1998).
28. O. Guittet, B. Roy, M. Lepoivre, Cell. Mol. Life Sci. 55, 1054 (1999).
29. M. Fontecave, Cell. Mol. Life Sci. 54, 684 (1998).
30. J. MacMicking, Q. W. Xie, C. Nathan, Annu. Rev. Immunol. 15, 323 (1997).
31. J. U. Igietseme et al., Infect. Immun. 66, 1282 (1998).
32. L. L. Perry, K. Feilzer, H. D. Caldwell, Infect. Immun. 66, 1265 (1998).
33. K. H. Ramsey et al., Infect. Immun. 66, 835 (1998).
34. M. Horn et al. Science 304, 728 (2004).
35. This work was supported by the Swedish Research Council and the European Union-Training and Mobility of Researchers iron-oxygen network. We thank Y. Cerenius for assistance at the 1711 beam-line at MAX-Lab.