Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme

Science

Volumn 303, Issue 5654, 2004, Pages 76-79

  Berkovitch, Frederick ^a   Nicolet, Yvain ^a   Wan, Jason T ^b   Jarrett, Joseph T ^b   Drennan, Catherine L ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; SULFUR;

BIOTINS;

ENZYMES;

BIOTIN SYNTHASE; RADICAL; S ADENOSYLMETHIONINE; SULFUR;

BIOLOGY; CRYSTAL STRUCTURE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME MECHANISM; ENZYME SUBSTRATE; ESCHERICHIA COLI; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; BINDING SITES; BIOTIN; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN; HYDROGEN BONDING; IRON; LIGANDS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; S-ADENOSYLMETHIONINE; SULFUR; SULFURTRANSFERASES;

ESCHERICHIA COLI; INSERTION SEQUENCES;

EID: 0346727529     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1088493     Document Type: Article

References (43)

1. P. A. Frey, S. J. Booker, Adv. Protein Chem. 58, 1 (2001).
2. J. Cheek, J. B. Broderick, J. Biol. Inorg. Chem. 6, 209 (2001).
3. J. T. Jarrett, Curr. Opin. Chem. Biol. 7, 174 (2003).
4. P. A. Frey, FASEB J. 7, 662 (1993).
5. P. A. Frey, G. H. Reed, Arch. Biochem. Biophys. 382, 6 (2000).
6. F. Escalettes, D. Florentin, B. Tse Sum Bui, D. Lesage, A. Marquet, J. Am. Chem. Soc. 121, 3571 (1999).
7. R. Benda et al., Biochemistry 41, 15000 (2002).
8. E. C. Duin et al., Biochemistry 36, 11811 (1997).
9. S. Ollagnier-de Choudens et al., Biochemistry 39, 4165 (2000).
10. S. Ollagnier-de Choudens, E. Mulliez, K. S. Hewiston, M. Fontecave, Biochemistry 41, 9145 (2002).
11. I. Sanyal, G. Cohen, D. H. Flint, Biochemistry 33, 3625 (1994).
12. B. Tse Sum Bui, D. Florentin, A. Marquet, R. Benda, A. X. Trautwein, FEBS Lett. 459, 411 (1999).
13. N. B. Ugulava, B. R. Gibney, J. T. Jarrett, Biochemistry 40, 8343 (2001).
14. N. B. Ugulava, K. K. Surerus, J. T. Jarrett, J. Am. Chem. Soc. 124, 9050 (2002).
15. B. Tse Sum Bui et al., FEBS Lett. 440, 226 (1998).
16. N. B. Ugulava, C. J. Sacanell, J. T. Jarrett, Biochemistry 40, 8352 (2001).
17. B. Tse Sum Bui et al., Biochemistry 42, 8791 (2003).
18. S. Ollagnier-de Choudens, E. Mulliez, M. Fontecave, FEBS Lett. 532, 465 (2002).
19. I. Sanyal, K. J. Gibson, D. H. Flint, Arch. Biochem. Biophys. 326, 48 (1996).
20. H. J. Sofia, G. Chen, B. G. Hetzler, J. F. Reyes-Spindola, N. E. Miller, Nucleic Acids Res. 29, 1097 (2001).
21. free is 30.0%. For a description of the structure elucidation and a table of data and refinement statistics, see the supporting online material.
22. A. G. Murzin et al., J. Mol. Biol. 247, 536 (1995).
23. M. M. Cosper, G. N. L. Jameson, M. K. Eidsness, B. H. Huynh, M. K. Johnson, FEBS Lett. 529, 332 (2002).
24. K. S. Hewitson, J. E. Baldwin, N. M. Shaw, P. L. Roach, FEBS Lett. 466, 372 (2000).
25. S. Ollagnier-de Choudens, Y. Sanakis, K. S. Hewiston, P. Roach, E. Munck, J. Biol. Chem. 277, 13449 (2002).
26. N. B. Ugulava, B. R. Gibney, J. T. Jarrett, Biochemistry 39, 5206 (2000).
27. M. Baranska, E. Gumienna-Kontecka, H. Kozlowski, L. M. Proniewicz, J. Inorg. Biochem. 92, 112 (2002).
28. S. Aoki, K. Iwaida, N. Hanamoto, M. Shiro, E. Kimura, J. Am. Chem. Soc. 124, 5256 (2002).
29. D. P. Fairlie et al., Inorg. Chem. 36, 1020 (1997).
30. K. S. Hewitson et al., J. Biol. Inorg. Chem. 7, 83 (2002).
31. C. Krebs, W. E. Broderick, T. F. Henshaw, J. B. Broderick, B. H. Huynh, J. Am. Chem. Soc. 124, 912 (2002).
32. C. J. Walsby, D. Ortillo, W. E. Broderick, J. B. Broderick, B. M. Hoffman, J. Am. Chem. Soc. 124, 11270 (2002).
33. M. M. Cosper et al., J. Am. Chem. Soc. 124, 14006 (2002).
34. A. Liu, A. Graslund, J. Biol. Chem. 275, 12367 (2000).
35. D. Padovani, F. Thomas, A. X. Trautwein, E. Mulliez, M. Fontecave, Biochemistry 40, 6713 (2001).
36. C. J. Walsby et al., J. Am. Chem. Soc. 124, 3143 (2002).
37. M. M. Cosper et al., Protein Sci. 12, 1573 (2003).
38. N. B. Ugulava, K. K. Frederick, J. T. Jarrett, Biochemistry 42, 2708 (2003).
39. F. Mancia et al., Structure 4, 339 (1996).
40. J. Masuda, N. Shibata, Y. Morimoto, T. Toraya, N. Yasuoka, Struct. Fold. Des. 8, 775 (2000).
41. R. Reitzer et al., Struct. Fold. Des. 7, 891 (1999).
42. W. L. DeLano, The PyMOL Molecular Graphics System at http://www.pymol. org (2002).
43. Supported by NIH grants R01-GM59175 (J.T.J.) and R01-GM65337 (C.L.D.), the Searle Scholars Program (C.L.D.), the Cecil and Ida Green Career Development Fund (C.L.D.), a Lester Wolfe Predoctoral Fellowship (F.B.), and a Cellular, Biochemical, and Molecular Sciences NIH training grant T32-GM07229 (J.T.W.). Data were collected at the National Synchrotron Light Source (NSLS), Advanced Light Source (ALS), and Stanford Synchrotron Radiation Laboratory (SSRL). Synchrotron facilities are funded by the U.S. Department of Energy (ALS 5.0.2, NSLS X25, SSRL), NIH National Center of Research Resources (NSLS X25), and National Institute of General Medical Sciences (NSLS X25). Coordinates and structure factors have been deposited in the Protein Data Bank with accession number 1R30.