Two structures of an N-hydroxylating flavoprotein monooxygenase: Ornithine hydroxylase from Pseudomonas aeruginosa

Journal of Biological Chemistry

Volumn 286, Issue 36, 2011, Pages 31789-31798

  Olucha, Jose ^a   Meneely, Kathleen M ^a   Chilton, Annemarie S ^a   Lamb, Audrey L ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BAEYER-VILLIGER MONOOXYGENASES; CLASS B; CO-SUBSTRATE; ELECTRON DONORS; HYDROXYLASES; MONOOXYGENASES; PRODUCT FORMATION; PSEUDOMONAS AERUGINOSA; ROSSMANN; SIDE-CHAINS; SIDEROPHORES; STRUCTURAL EVIDENCE; SUBSTRATE-BINDING DOMAINS;

BACTERIA; HYDROXYLATION; MOLECULAR OXYGEN; REACTION INTERMEDIATES; SUBSTRATES;

AMINO ACIDS;

FLAVINE ADENINE NUCLEOTIDE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; ORNITHINE; ORNITHINE HYDROXYLASE; OXYGEN; PYOVERDINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

ARTICLE; CATALYSIS; COMPETITIVE INHIBITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME METABOLISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROXYLATION; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PSEUDOMONAS AERUGINOSA; ROSSMANN LIKE DINUCLEOTIDE BINDING DOMAIN; SUBSTRATE BINDING DOMAIN;

CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; FLAVIN-ADENINE DINUCLEOTIDE; MIXED FUNCTION OXYGENASES; NADP; ORNITHINE; OXIDATION-REDUCTION; OXYGENASES; PROTEIN CONFORMATION; PSEUDOMONAS AERUGINOSA; SUBSTRATE SPECIFICITY;

PSEUDOMONAS AERUGINOSA;

EID: 80052395555     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.265876     Document Type: Article

References (36)

1. Meneely, K. M., and Lamb, A. L. (2007) Biochemistry 46, 11930-11937
2. Van Berkel, W. J., Kamerbeek, N. M., and Fraaije, M. W. (2006) J. Biotechnol. 124, 670-689
3. Ge, L., and Seah, S. Y. (2006) J. Bacteriol. 188, 7205-7210
4. Meneely, K. M., Barr, E. W., Bollinger, J. M., Jr., and Lamb, A. L. (2009) Biochemistry 48, 4371-4376
5. Chocklett, S. W., and Sobrado, P. (2010) Biochemistry 49, 6777-6783
6. Mayfield, J. A., Frederick, R. E., Streit, B. R., Wencewicz, T. A., Ballou, D. P., and DuBois, J. L. (2010) J. Biol. Chem. 285, 30375-30388
7. Thariath, A., Socha, D., Valvano, M. A., and Viswanatha, T. (1993) J. Bacteriol. 175, 589-596
8. Thariath, A. M., Fatum, K. L., Valvano, M. A., and Viswanatha, T. (1993) Biochim. Biophys. Acta 1203, 27-35
9. Sheng, D., Ballou, D. P., and Massey, V. (2001) Biochemistry 40, 11156-11167
10. Krueger, S. K., and Williams, D. E. (2005) Pharmacol. Ther. 106, 357-387
11. Mirza, I. A., Yachnin, B. J., Wang, S., Grosse, S., Bergeron, H., Imura, A., Iwaki, H., Hasegawa, Y., Lau, P. C., and Berghuis, A. M. (2009) J. Am.Chem. Soc. 131, 8848-8854
12. Alfieri, A., Malito, E., Orru, R., Fraaije, M. W., and Mattevi, A. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 6572-6577
13. Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L., and Clardy, J. (1993) J. Mol. Biol. 229, 105-124
14. Kabsch, W. (2010) Acta Crystallogr. D 66, 125-132
15. Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., Mc- Coy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., and Zwart, P. H. (2010) Acta Crystallogr. D 66, 213-221
16. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. D 53, 240-255
17. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D 60, 2126-2132
18. McCoy, A. J., Grosse-Kunstleve, R. W., Storoni, L. C., and Read, R. J. (2005) Acta Crystallogr. D 61, 458-464
19. Laskowski, R., MacArthur, M., Moss, D., and Thornton, J. (1993) J. Appl. Crystallogr. 26, 283-291
20. Kleywegt, G. J., and Jones, T. A. (1997) Methods Enzymol. 277, 525-545
21. DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific LLC, San Carlos, CA
22. Bond, C. S. (2003) Bioinformatics 19, 311-312
23. Reynolds, C., Damerell, D., and Jones, S. (2009) Bioinformatics 25, 413-414
24. Jones, S., and Thornton, J. M. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 13-20
25. Krissinel, E., and Henrick, K. (2004) Acta Crystallogr. D 60, 2256-2268
26. Dym, O., and Eisenberg, D. (2001) Protein Sci. 10, 1712-1728
27. Kamerbeek, N. M., Fraaije, M. W., and Janssen, D. B. (2004) FEBS Lett. 271, 2107-2116
28. Cho, H. J., Cho, H. Y., Kim, K. J., Kim, M. H., Kim, S. W., and Kang, B. S. (2011) J. Struct. Biol. 175, 39-48
29. Eswaramoorthy, S., Bonanno, J. B., Burley, S. K., and Swaminathan, S. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 9832-9837
30. Orru, R., Pazmiño, D. E., Fraaije, M. W., and Mattevi, A. (2010) J. Biol. Chem. 285, 35021-35028
31. Malito, E., Alfieri, A., Fraaije, M. W., and Mattevi, A. (2004) Proc. Natl. Acad. Sci. U.S.A. 101, 13157-13162
32. Beaty, N. B., and Ballou, D. P. (1980) J. Biol. Chem. 255, 3817-3819
33. Beaty, N. B., and Ballou, D. P. (1981) J. Biol. Chem. 256, 4619-4625
34. Gatti, D. L., Palfey, B. A., Lah, M. S., Entsch, B., Massey, V., Ballou, D. P., and Ludwig, M. L. (1994) Science 266, 110-114
35. Moran, G. R., Entsch, B., Palfey, B. A., and Ballou, D. P. (1996) Biochemistry 35, 9278-9285
36. Palfey, B. A., Moran, G. R., Entsch, B., Ballou, D. P., and Massey, V. (1999) Biochemistry 38, 1153-1158