A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis

Journal of Biological Chemistry

Volumn 281, Issue 48, 2006, Pages 36929-36936

  Yu, Yamei ^a   Liang, Yu He ^a   Brostromer, Erik ^a   Quan, Jun Min ^a   Panjikar, Santosh ^b   Dong, Yu Hui ^c   Su, Xiao Dong ^a  

^a PEKING UNIVERSITY   (China)

^b DESY   (Germany)

^c INSTITUTE OF HIGH ENERGY PHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ACETATE ION; GLUTAMIC ACID; HISTIDINE DEGRADATION; X RAY FLUORESCENCE;

ACETIC ACID; BIODEGRADATION; CATALYSIS; CRYSTAL STRUCTURE; ENZYMES; HYDROLYSIS; SUBSTRATES; ZINC;

BACTERIA;

4 IMIDAZOLEACETIC ACID; ARGININE; ASPARTIC ACID; BACTERIAL ENZYME; CYTOSINE DEAMINASE; GLUTAMIC ACID; HISTIDINE; HYDROLASE; IMIDAZOLONEPROPIONASE; METAL ION; TRIOSEPHOSPHATE ISOMERASE; TYROSINE; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CRYSTAL STRUCTURE; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ANALYSIS; X RAY FLUORESCENCE;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 33845986728     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M607703200     Document Type: Article

References (37)

1. Revel, H. R., and Magasanik, B. (1958) J. Biol. Chem. 233, 930-935
2. Brown, D. D., Silva, O. L., Gardiner, R. C., and Silverman, M. (1960) J. Biol. Chem. 235, 2058-2062
3. Chasin, L. A., and Magasanik, B. (1968) J. Biol. Chem. 243, 5165-5178
4. Kimhi, Y., and Magasanik, B. (1970) J. Biol. Chem. 245, 3545-3548
5. Oda, M., Sugishita, A., and Furukawa, K. (1988) J. Bacteriol. 170, 3199-3205
6. Yoshida, K., Sano, H., Seki, S., Oda, M., Fujimura, M., and Fujita, Y. (1995) Microbiology (Read.) 141, 337-343
7. Schwede, T. F., Badeker, M., Langer, M., Retey, J., and Schulz, G. E. (1999) Protein Eng. 12, 151-153
8. Schwede, T. F., Retey, J., and Schulz, G. E. (1999) Biochemistry 38, 5355-5361
9. Kessler, D., Retey, J., and Schulz, G. E. (2004) J. Mol. Biol. 342, 183-194
10. Smith, G. R., Halpern, Y. S., and Magasanik, B. (1971) J. Biol. Chem. 246, 3320-3329
11. Rao, D. R., and Greenberg, D. M. (1960) Biochim. Biophys. Acta 43, 404-418
12. Snyder, S. H., Silva, O. L., and Kies, M. W. (1961) J. Biol. Chem. 236, 2996-2998
13. Holm, L., and Sander, C. (1997) Proteins 28, 72-82
14. Doublie, S. (1997) Methods Enzymol. 276, 523-530
15. Yu, Y., Li, L., Zheng, X., Liang, Y. H., and Su, X. D. (2006) Biochim. Biophys. Acta 1764, 153-156
16. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
17. Panjikar, S., Parthasarathy, V., Lamzin, V. S., Weiss, M. S., and Tucker, P. A. (2005) Acta Crystallogr. Sect. D Biol. Crystallogr. 61, 449-457
18. Cowtan, K. (1994) Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31, 34-38
19. Sheldrick, G. M., Hauptman, H. A., Weeks, C. M., Miller, R., and Usón, I. (2001) in International Tables for Crystallography (Rossmann, M. G., and Arnold, E., eds) pp. 333-351, IUCr and Kluwer Academic Publishers, Norwell, MA
20. Schneider, T. R., and Sheldrick, G. M. (2002) Acta Crystallogr. Sect. D Biol. Crystallogr. 58, 1772-1779
21. Hao, Q. (2004) J. Appl. Crystallogr. 37, 498-499
22. Sheldrick, G. M. (2002) Z. Kristallogr. 217, 644-650
23. Perrakis, A., Sixma, T. K., Wilson, K. S., and Lamzin, V. S. (1997) Acta Crystallogr. Sect. D Biol. Crystallogr. 53, 448-455
24. Morris, R. J., Zwart, P. H., Cohen, S., Fernandez, F. J., Kakaris, M., Kirillova, O., Vonrhein, C., Perrakis, A., and Lamzin, V. S. (2004) J. Synchrotron Radiat. 11, 56-59
25. Jones, T. A., Bergdoll, M., and Kjeldgaard, M. (1990) in Crystallographic and Modeling Methods in Molecular Design (Bugg, C., and Ealick, S., eds) pp. 189-195, Springer-Verlag Press, Berlin
26. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905-921
27. Okabe, N., and Hayashi, T. (1999) Acta Crystallogr. Sect. C Cryst. Struct. Commun. 55, 1142-1144
28. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
29. Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) Nucleic Acids Res. 25, 4876-4882
30. Gouet, P., Courcelle, E., Stuart, D. I., and Metoz, F. (1999) Bioinformatics 15, 305-308
31. Kabsch, W., and Sander, C. (1983) Biopolymers 22, 2577-2637
32. Lopez, R., Silventoinen, V., Robinson, S., Kibria, A., and Gish, W. (2003) Nucleic Acids Res. 31, 3795-3798
33. Dietmann, S., Park, J., Notredame, C., Heger, A., Lappe, M., and Holm, L. (2001) Nucleic Acids Res. 29, 55-57
34. Ireton, G. C., McDermott, G., Black, M. E., and Stoddard, B. L. (2002) J. Mol. Biol. 315, 687-697
35. Porter, D. J. (2000) Biochim. Biophys. Acta 1476, 239-252
36. Wilson, D. K., Rudolph, F. B., and Quiocho, F. A. (1991) Science 252, 1278-1284
37. Bond, C. S. (2003) Bioinformatics (Oxf.) 19, 311-312