Haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 refined at 1.15 Å resolution

Acta Crystallographica Section D: Biological Crystallography

Volumn 55, Issue 7, 1999, Pages 1273-1290

  Ridder, Ivo S ^a   Rozeboom, Henriëtte J ^a   Dijkstra, Bauke W ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE; HALOALKANE DEHALOGENASE; HYDROLASE; SOLVENT;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GRAM NEGATIVE AEROBIC RODS AND COCCI; HYDROGEN BOND; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

CHLORIDES; CRYSTALLOGRAPHY, X-RAY; GRAM-NEGATIVE AEROBIC BACTERIA; HYDROGEN BONDING; HYDROLASES; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; SOLVENTS;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; XANTHOBACTER AUTOTROPHICUS;

EID: 0033166637     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S090744499900534X     Document Type: Article

References (66)

1. Abola, E. E., Sussman, J. L., Prilusky, J. & Manning, N. O. (1997). Methods Enzymol. 277, 556-571.
2. Allen, E. H. S., Bellard, S., Brice, M. D., Cartwright, B. A., Doubleday, A., Higgs, H., Hummelink, T., Hummelink-Peters, B. G., Kennard, O., Motherwell, W. D. S., Rodgers, J. R. & Watson, D. G. (1979). Acta Crvst. B35, 2331-2339.
3. Blundell, T. L. & Johnson, L. N. (1976). Protein Crystallography, edited by B. Horecker, N. O. Kaplan, J. Marmur & H. A. Scheraga. New York: Academic Press.
4. Brünger, A. T. (1992a). Nature (London). 355, 472-475.
5. Brüdnger, A. T. (1992b). X-PLOR Version 3.1. A System for X-ray Crystallography and NMR. New Haven, Connecticut: Yale University Press.
6. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763,
7. Dauter, Z., Lamzin, V. S. & Wilson, K. S. (1997). Curr. Opin. Struct. Biol. 7, 681-688.
8. Derewenda, Z. S., Lee, L. & Derewenda, U. (1995). J. Mol. Biol, 252, 248-262.
9. Desiraju, G. R. (1991). Acc. Chem. Res. 24, 290-296.
10. Desiraju, G. R. (1996). Acc. Chem. Res. 29, 441-449.
11. Engh, R. A. & Huber, R. (1991). Acta Cryst. A47, 392-400.
12. Esnouf, R. M. (1997). J. Mol. Graph, 15, 133-138.
13. Fabiola, G. F., Krishnaswamy, S., Nagarajan, V. & Pattabhi, V. (1997). Acta Cryst. D53, 316-320.
14. Franken, S. M., Rozeboom, H. J., Kalk, K. H. & Dijkstra, B. W. (1991). EMBO J. 10, 1297-1302.
15. Gliubich, F., Gazerro, M., Zanotti, G., Delbono, S., Bombieri, G. & Berni, R. (1996). J. Biol. Chem. 271, 21054-21061.
16. Hirshfeld, F. L. & Rabinovich, D. (1973). Acta Cryst. A29, 510-513.
17. Hooft, R. W. W., Vriend, G., Sander, C. & Abola, E. E. (1996). Nature (London). 381, 272.
18. Janssen, D. B., Scheper, A., Dijkhuizen, L. & Witholt, B. (1985). Appl. Environm. Microbiol. 49, 673-677.
19. Janssen, D. B., Van den Wijngaard, A. J., Van der Waarde, J. J. & Oldenhuis, R. (1991). On-site Bioreclamation, pp. 92-122, Boston: Butterworth-Heinemann.
20. Jeffrey, G. A. & Sänger, W. (1991). Hydrogen Bonding in Biological Structures. Berlin: Heidelberg; New York: Springer-Verlag.
21. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.
22. Kabsch, W. & Sander, C. (1983). Biopolymers, 22, 2577-2637.
23. Keuning, S., Janssen, D. B. & Witholt, B. (1985). J. Bacteriol. 163, 635-639.
24. Kleywegt, G. J. & Jones, T. A. (1994). Acta Cryst. D50, 178-185.
25. Kroon, J. & Kanters, J. A. (1974). Nature (London). 248, 667-669.
26. Krooshof, G. H., Ridder, I. S., Tepper, A. W. J. W., Vos, G. J., Rozeboom, H. J., Kalk, K. H., Dijkstra, B. W. & Janssen, D. B. (1998). Biochemistry, 37, 15013-15023.
27. Lamzin, V. S. & Wilson, K. S. (1993). Acta Cryst. D49, 129-147.
28. Lamzin, V. S. & Wilson, K. S. (1997). Methods Enzymol. 277, 269-305.
29. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
30. Leonard, G. A., McAuley-Hecht, K., Brown, T. & Hunter, W. N. (1995). Acta Cryst. D51, 136-139.
31. Luzzati, V. (1952). Acta Cryst. 5, 802-810.
32. MacArthur, M. W. & Thornton, J. M. (1996). J. Mol. Biol. 264, 1180-1195.
33. McDonald, I. K. & Thornton, J. M. (1994). J. Mol. Biol. 238, 777-793.
34. Moews, P. C. & Kretsinger, R. H. (1975). J. Mol. Biol. 91, 201-228.
35. Morris, A. L., MacArthur, M. W., Hutchinson, E. G. & Thornton, J. M. (1992). Proteins Struct. Funct. Genet. 12, 345-364.
36. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1997). Acta Cryst. D53, 240-255.
37. Nardini, M. (1998). Personal communication.
38. Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., Sussman, J. L., Verschueren, K. H. G. & Goldman, A. (1992). Protein Eng. 5, 197-211.
39. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
40. Pikkemaat, M. G., Ridder, I. S., Rozeboom, H. J., Kalk, K. H., Dijkstra, B. W. & Janssen, D. B. (1999). In preparation.
41. Pries, F., Kingma, J., Pentenga, M., Van Pouderoyen, G., Jeronimus Stratingh, C. M., Bruins, A. P. & Janssen, D. B. (1994). Biochemistry, 33, 1242-1247.
42. Ramachandran, G. N. & Sasisekharan, V. (1968). Adv. Prot. Chem. 23, 283-437.
43. Read, R. J. (1986). Acta Cryst. A42, 140-149.
44. Rozeboom, H. J., Kingma, J., Janssen, D. B. & Dijkstra, B. W. (1988). J. Mol. Biol. 200, 611-612.
45. Schanstra, J. P. & Janssen, D. B. (1996). Biochemistry, 35, 5624-5632.
46. Schanstra, J. P., Kingma, J. & Janssen, D. B. (1996). J. Biol. Chem. 271, 14747-14753.
47. Schanstra, J. P., Ridder, I. S., Heimeriks, G. J., Rink, R., Poelarends, G. J., Kalk, K. H., Dijkstra, B. W. & Janssen, D. B. (1996). Biochemistry, 35, 13186-13195,
48. Sevcik, J., Dauter, Z., Lamzin, V. S. & Wilson, K. S. (1996). Acta Cryst. D52, 327-344.
49. Sheldrick, G. M. (1990). Acta Cryst. A46, 467-473.
50. Sheldrick, G. M. & Schneider, T. R. (1997). Methods Enzymol. 277, 319-343.
51. Steiner, T. (1997). J. Chem. Soc. Chem. Commun. pp. 727-734.
52. Steiner, T. (1998). Acta Cryst. B54, 456-463.
53. Stucki, G. & Thüer, M. (1994). Appl. Microbiol. Biotechnol. 42, 167-172.
54. Stucki, G. & Thüer, M. (1995). Environ. Sci. Technol. 29, 2339-2345.
55. Taylor, R. & Kennard, O. (1982). J. Am. Chem. Soc. 104, 5063-5070.
56. Tronrud, D. E. (1997). Methods Enzymol. 277, 306-319.
57. Van Mourik, T. & Van Duijneveldt, E B. (1995). J. Mol. Struct. (THEOCHEM). 341, 63-73.
58. Verschueren, K. H. G., Franken, S. M., Rozeboom, H. J., Kalk, K. H. & Dijkstra, B. W. (1993). J. Mol. Biol. 232, 856-872.
59. Verschueren, K. H. G., Kingma, J., Rozeboom, H. J., Kalk, K. H., Janssen, D. B. & Dijkstra, B. W. (1993). Biochemistry, 32, 9031-9037.
60. Verschueren, K. H. G., Seljée, F., Rozeboom, H. J., Kalk, K. H. & Dijkstra, B. W. (1993). Nature (London). 363, 693-698.
61. Walsh, M. A., Schneider, T. R., Sieker, L. C., Dauter, Z., Lamzin, V. S. & Wilson, K. S. (1998). Acta Cryst. D54, 522-546.
62. Watkin, A. (1994). Acta Cryst. A50, 411-437.
63. Wilson, A. J. C. (1942). Nature (London). 150, 152.
64. Wilson, A. J. C. (1973). Acta Cryst. B29, 1488-1490.
65. Wilson, A. J. C. (1976). Acta Cryst. A32, 781-783.
66. Wilson, K. S., Dauter, Z., Lamzin, V. S., Walsh, M., Wodak, S., Richelle, J., Pontius, J., Vaguine, A, Hooft, R. W. W., Sander, C., Vriend, G., Thornton, J. M., Laskowski, R. A., MacArthur, M. W., Dodson, E. J., Murshudov, G., Oldfield, T. J., Kaptein, R. & Rullmann, J. A. C. (1998). J. Mol. Biol. 276, 417-436.