The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: The first crystal structure of a type II Baeyer-Villiger monooxygenase

Acta Crystallographica Section D: Biological Crystallography

Volumn 71, Issue , 2015, Pages 2344-2353

  Isupov, Michail N ^a   Schröder, Ewald ^a   Gibson, Robert P ^a   Beecher, Jean ^a   Donadio, Giuliana ^a   Saneei, Vahid ^a   Dcunha, Stephlina A ^a   Mcghie, Emma J ^a   Sayer, Christopher ^a   Davenport, Colin F ^a   Lau, Peter C ^b   Hasegawa, Yoshie ^c   Iwaki, Hiroaki ^c   Kadow, Maria ^d   Balke, Kathleen ^d   Bornscheuer, Uwe T ^d   Bourenkov, Gleb ^e   Littlechild, Jennifer A ^a  

^a UNIVERSITY OF EXETER   (United Kingdom)

^b NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^c KANSAI UNIVERSITY   (Japan)

^d UNIVERSITY OF GREIFSWALD   (Germany)

^e EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

FMN dependent monooxygenase; industrial biocatalysis; protein structure

Indexed keywords

3,6-DIKETOCAMPHANE MONOOXYGENASE; BACTERIAL PROTEIN; FLAVINE MONONUCLEOTIDE; FLAVINE MONONUCLEOTIDE REDUCTASE; OXYGENASE;

AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVE SITE; GENETICS; METABOLISM; MOLECULAR GENETICS; MOLECULAR MODEL; PLASMID; PROTEIN CONFORMATION; PROTEIN FOLDING; PSEUDOMONAS PUTIDA; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; FLAVIN MONONUCLEOTIDE; FMN REDUCTASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXYGENASES; PLASMIDS; PROTEIN CONFORMATION; PROTEIN FOLDING; PSEUDOMONAS PUTIDA; SEQUENCE ALIGNMENT;

EID: 84946594308     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004715017939     Document Type: Article

References (67)

1. Alphand, V., Carrea, G., Wohlgemuth, R., Furstoss, R., & Woodley, J. M. (2003). Trends Biotechnol. 21, 318-323.
2. Andreeva, A., Howorth, D., Chothia, C., Kulesha, E., & Murzin, A. G. (2014). Nucleic Acids Res. 42, D310-D314.
3. Aufhammer, S. W., Warkentin, E., Berk, H., Shima, S., Thauer, R. K., & Ermler, U. (2004). Structure, 12, 361-370.
4. Aufhammer, S. W., Warkentin, E., Ermler, U., Hagemeier, C. H., Thauer, R. K., & Shima, S. (2005). Protein Sci. 14, 1840-1849.
5. Baeyer, A., & Villiger, V. (1899). Ber. Dtsch. Chem. Ges. 32, 3625-3633.
6. Balke, K., Kadow, M., Mallin, H., Sass, S., & Bornscheuer, U. T. (2012). Org. Biomol. Chem. 10, 6249-6265.
7. Banner, D.W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., & Wilson, I. A. (1976). Biochem. Biophys. Res. Commun. 72, 146-155.
8. Beecher, J., & Willetts, A. (1998). Tetrahedron Asymmetry, 9, 1899-1916.
9. Bonanno, J. B. et al. (2005). J. Struct. Funct. Genomics, 6, 225-232.
10. Bornscheuer, U. T., Huisman, G., Kazlauskas, R. J., Lutz, S., Moore, J., & Robins, K. (2012). Nature (London), 485, 185-194.
11. Bricogne, G., Blanc, E., Brandl, M., Flensburg, C., Keller, P., Paciorek, P., Roversi, P., Sharff, A., Smart, O., Vonrhein, C., & Womack, T. (2015). BUSTER v.2.10.2. Cambridge: Global Phasing Ltd.
12. Campbell, Z. T., Weichsel, A., Montfort, W. R., & Baldwin, T. O. (2009). Biochemistry, 48, 6085-6094.
13. Conrad, H. E., Dubus, R., Namtvedt, M. J., & Gunsalus, I. C. (1965). J. Biol. Chem. 240, 495-503.
14. Cowtan K. (2010). Acta Cryst. D66, 470-478.
15. Dauter Z., Dauter, M., & Rajashankar, K. R. (2000). Acta Cryst. D56, 232-237.
16. DeLano, W. L. (2002). PyMOL. http://www.pymol.org.
17. Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
18. Eswaramoorthy, S., Bonanno, J. B., Burley, S. K., & Swaminathan, S. (2006). Proc. Natl Acad. Sci. USA, 103, 9832-9837.
19. Fisher, A. J., Thompson, T. B., Thoden, J. B., Baldwin, T. O., & Rayment, I. (1996). J. Biol. Chem. 271, 21956-21968.
20. Gagnon, R., Grogan, G., Levitt, M. S., Roberts, S. M., Wan, P.W. H., & Willetts, A. J. (1994). J. Chem. Soc. Perkin Trans. 1, pp. 2537-2543.
21. Gagnon, R., Grogan, G., Roberts, S. M., Villa, R., & Willetts, A. J. (1995). J. Chem. Soc. Perkin Trans. 1, pp. 1505-1511.
22. Grogan, G., Roberts, S., Wan, P., & Willetts, A. J. (1993). Biotechnol. Lett. 15, 913-918.
23. Grogan, G., Roberts, S., Wan, P., & Willetts, A. (1994). Biotechnol. Lett. 16, 1173-1178.
24. Grogan, G., Roberts, S. M., & Willetts, A. J. (1992). Biotechnol. Lett. 14, 1125-1130.
25. Grogan G., Roberts, S., & Willetts, A. J. (1993). J. Chem. Soc. Chem. Commun., pp. 699-701.
26. Isupov M. N., & Lebedev, A. A. (2008). Acta Cryst. D64, 90-98.
27. Jones, K. H., Smith, R. T., & Trudgill, P. W. (1993). J. Gen. Microbiol. 139, 797-805.
28. Jones T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.
29. Kabsch W. (2010). Acta Cryst. D66, 125-132.
30. Kadow, M., Balke, K., Willetts, A., Bornscheuer, U. T., & Backvall, J. E. (2014). Appl. Microbiol. Biotechnol. 98, 3975-3986.
31. Kadow, M., Loschinski, K., Sass, S., Schmidt, M., & Bornscheuer, U. T. (2012). Appl. Microbiol. Biotechnol. 96, 419-429.
32. Kelly, D. R. (1996). Tetrahedron Asymmetry, 7, 1149-1152.
33. Krow, G. R. (1993). Org. React. 43, 251-798.
34. Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
35. Laskowski, R. A., & Swindells, M. B. (2011). J. Chem. Inf. Model. 51, 2778-2786.
36. Lebedev A. A., Vagin, A. A., & Murshudov, G. N. (2008). Acta Cryst. D64, 33-39.
37. Lebedev A. A., Young, P., Isupov, M. N., Moroz, O. V., Vagin, A. A., & Murshudov, G. N. (2012). Acta Cryst. D68, 431-440.
38. LeGall, J., Bertland, A. U., Namtvedt, M. J., & Conrad, H. E. (1963). Fed. Proc. 22, 295.
39. Leisch, H., Morley, K., & Lau, P. C. K. (2011). Chem. Rev. 111, 4165-4222.
40. Li, L., Liu, X., Yang, W., Xu, F., Wang, W., Feng, L., Bartlam, M., Wang, L., & Rao, Z. (2008). J. Mol. Biol. 376, 453-465.
41. Lilly, M. D., Chauhan, R., French, C., Gyamerah, M., Hobbs, G. R., Humphrey, A., Isupov, M., Littlechild, J. A., Mitra, R. K., Morris, K. G., Rupprecht, M., Turner, N. J., Ward, J. M., Willetts, A. J., & Woodley, J. (1996). Ann. N. Y. Acad. Sci. 782, 513-525.
42. Littlechild, J. A., Guy, J., Connelly, S., Mallett, L., Waddell, S., Rye, C. A., Line, K., & Isupov, M. (2007). Biochem. Soc. Trans. 35, 1558-1563.
43. Malito, E., Alfieri, A., Fraaije, M. W., & Mattevi, A. (2004). Proc. Natl Acad. Sci. USA, 101, 13157-13162.
44. McGhie, E. J. (1998). PhD Thesis, University of Exeter.
45. McGhie, E. J., Isupov, M. N., Schroder, E., & Littlechild, J. A. (1998). Acta Cryst. D54, 1035-1038.
46. McGhie, E., & Littlechild, J. (1996). Biochem. Soc. Trans. 24, 29S.
47. McNicholas S., Potterton, E., Wilson, K. S., & Noble, M. E. M. (2011). Acta Cryst. D67, 386-394.
48. Murshudov G. N., Skubak, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F., & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
49. Opperman, D. J., Sewell, B. T., Litthauer, D., Isupov, M. N., Littlechild, J. A., & van Heerden, E. (2010). Biochem. Biophys. Res. Commun. 393, 426-431.
50. Otwinowski Z. (1991). Proceedings of the CCP4 Study Weekend. Isomorphous Replacement and Anomalous Scattering, edited by W. Wolf, P. R. Evans & A. G. W. Leslie, pp. 80-86. Warrington: Daresbury Laboratory.
51. Otwinowski, Z., & Minor, W. (1997). Methods Enzymol. 276, 307-326.
52. Pannu N. S., Murshudov, G. N., Dodson, E. J., & Read, R. J. (1998). Acta Cryst. D54, 1285-1294.
53. Reetz, M. T. (2013). J. Am. Chem. Soc. 135, 12480-12496.
54. Robert, X., & Gouet, P. (2014). Nucleic Acids Res. 42, W320-W324.
55. Roberts, S. M., & Wan, P. W. H. (1998). J. Mol. Catal. B Enzym. 4, 111-136.
56. Røhr, A. K., Asmund, K., Hersleth, H., & Andersson, K. K. (2010). Angew. Chem. Int. Ed. 49, 2324-2327.
57. Shaham, M., Chakrabarty, A.M., & Gunsalus, I. C. (1973). J. Bacteriol. 116, 944-949.
58. Sheldrick G. M. (2010). Acta Cryst. D66, 479-485.
59. Sucharitakul, J., Chaiyen, P., Entsch, B., & Ballou, D. P. (2006). J. Biol. Chem. 281, 17044-17053.
60. Vagin, A. A., Murshudov, G. N., & Strokopytov, B. V. (1998). J. Appl. Cryst. 31, 98-102.
61. Vagin A., & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
62. Vaguine A. A., Richelle, J., & Wodak, S. J. (1999). Acta Cryst. D55, 191-205.
63. Vivoli, M., Ayres, E., Beaumont, E., Isupov, M. N., & Harmer, N. J. (2014). IUCrJ, 1, 28-38.
64. Wierenga, R. K. (2001). FEBS Lett. 492, 193-198.
65. Winn M. D. et al. (2011). Acta Cryst. D67, 235-242.
66. Winter G., Lobley, C. M. C., & Prince, S. M. (2013). Acta Cryst. D69, 1260-1273.
67. Wohlgemuth, R. (2010). Curr. Opin. Biotechnol. 21, 713-724.