The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product glutamate, and (ii) its end-product inhibitor, L-tryptophan

Proceedings of the National Academy of Sciences of the United States of America

Volumn 98, Issue 11, 2001, Pages 6021-6026

  Spraggon, Glen ^a   Kim, Choel ^b   Nguyen Huu, Xuong ^b   Yee, Muh Ching ^c   Yanofsky, Charles ^c   Mills, Stanley E ^b  

^a Novartis Reserarch Foundation   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c STANFORD UNIVERSITY   (United States)

Author keywords

Anthranilate biosynthesis; Anthranilate synthase x ray structure; Tryptophan feedback inhibition

Indexed keywords

ANTHRANILIC ACID; BACTERIAL ENZYME; CHORISMIC ACID; ESTER DERIVATIVE; GLUTAMIC ACID; GLUTAMINE; GLUTAMYL THIOESTER; NITROGEN; OLIGOMER; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME MECHANISM; FEEDBACK SYSTEM; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; SERRATIA MARCESCENS; SULFOLOBUS SOLFATARICUS;

AMINO ACID SEQUENCE; ANTHRANILATE SYNTHASE; ANTHRANILIC ACIDS; BASE SEQUENCE; BINDING SITES; CHORISMIC ACID; CRYSTALLOGRAPHY, X-RAY; CYCLOHEXENES; DNA, BACTERIAL; GLUTAMIC ACID; GLUTAMINE; LYASES; MOLECULAR SEQUENCE DATA; NITROGENOUS GROUP TRANSFERASES; OLIGOPEPTIDES; PROTEIN STRUCTURE, SECONDARY; SERRATIA MARCESCENS; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

BACTERIA (MICROORGANISMS); ENTERIC BACTERIA; SERRATIA MARCESCENS; SULFOLOBUS SOLFATARICUS;

EID: 0035933197     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.111150298     Document Type: Article

References (43)

1. Morollo, A. A. & Bauerle, R. (1993) Proc. Natl. Acad. Sci. USA 90, 9983-9987.
2. Zalkin, H. & Hwang, L. H. (1971) J. Biol. Chem. 246, 6899-6907.
3. Zalkin, H. (1993) Adv. Enzymol. Relat. Areas Mol. Biol. 66, 203-309.
4. Tesmer, J. J., Klem, T. J., Deras, M. L., Davisson, V. J. & Smith, J. L. (1996) Nat. Struct. Biol. 3, 74-86.
5. Bauerle, R., Hess, J. & French, S. (1987) Methods Enzymol. 142, 366-386.
6. Robb, F. T., Hutchinson, M. A. & Belser, W. H. (1971) J. Biol. Chem. 246, 6908-6912.
7. Yanofsky, C., Miles, E. W., Bauerle, R. & Kirschner, K. (1999) in Encyclopedia of Molecular Biology (Wiley, New York), Vol. 4, pp. 2676-2687.
8. Tolbert, W. D., Chatterji, S., Bauerle, R. & Kretsinger, S. (1999) Acta Crystallogr. D55, 305-306.
9. Knöchel, T., Ivens, A., Hester, G., Gonzalez, A., Bauerle, R., Wilmanns, M., Kirschner, K. & Jansonius, J., N. (1999) Proc. Natl. Acad. Sci. USA 96, 9479-9484.
10. Segerer, A. & Stetter, K. O. in Bergeyt's Manual of Systematic Bacteriology (Williams & Wilkins, Baltimore), Vol. 3, pp. 2250-2251.
11. Miozarri, G. & Yanofsky, C. (1979) Nature (London) 277, 486-489.
12. Tso, J. Y., Hermodson, M. A. & Zalkin, H. (1980) J. Biol. Chem. 255, 1451-1457.
13. Paluh, J. L. & Yanofsky, C. (1996) Nucleic Acids Res. 14, 7851-7860.
14. Vogel, H. J. & Bonner, D. M. (1957) J. Biol. Chem. 218, 97-106.
15. Otwinowski, Z. & Minor, W. (1997) Methods Enzymol. 276, 307-326.
16. Leslie, A., A. W. (1992) Jnt. CCP4/ESF-EACMB Newslett. Protein Crystallogr. 26.
17. Collaborative Computing Project Number 4 (1994) Acta Crystallogr. D50, 760-763.
18. Navaza, J. (1994) Acta. Crystallogr. A50, 157-163.
19. Read, R. J. (1986) Acta. Crystallogr. A42, 140-149.
20. Cowtan, K. (1994) Jnt. CCP4/ESF-EACMB Newslett. Protein Crystallogr. 31, 34.
21. Brünger, 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., et al. (1998) Acta Crystallogr. D54, 905-921.
22. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1991) Acta Crystallogr. D53, 240-255.
23. Perrakis, A., Sixma, T. K., Wilson, K. S. & Lamzin, V. S. (1997), in Recent Advances in Phasing, eds. Wilson, K. S., Davies, G., Ashton, A. W. & Bailey, S. (SERC, Daresbury Laboratories, Warrington, U.K.), pp. 82-91.
24. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. (1991) Acta Crystallogr. A47, 110-119.
25. Brünger, A. T. (1997) Methods Enzymol. 277, 366-396.
26. Murzin, A. G., Brenner, S. E., Hubbard, T. & Chothia, C. (1995) J. Mol. Biol. 247, 536-540.
27. Thoden, J. B., Holden, H. M., Wesenberg, G., Raushel, F. M. & Rayment, I. (1997) Biochemistry 36, 6305-6316.
28. Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harrel, M., Remington, S. J., Silman, I., Schrag, J., et al. (1992) Protein Eng. 5, 197-211.
29. Richards, F. M. (1977) Annu. Rev. Biophys. Bioeng. 6, 151-176.
30. Thoden, J. B., Miran, S. G., Howard, A. J., Phillips, J. C., Raushel, F. M. & Holden, H. M. (1998) Biochemistry 37, 8825-8831.
31. Thoden, J. B., Huang, X., Raushel, F. M. & Holden, H. M. (1999) Biochemistry 38, 16158-16166.
32. Raushel, F. M., Thoden, J. B. & Holden, H., M. (1999) Biochemistry 38, 7891-7899.
33. Thoden, J. B., Wesenberg, G., Raushel, F. M. & Holden, H. M. (1999) Biochemistry 38, 2347-2357.
34. Caligiuri, M. G. & Bauerle, R. (1991) J. Biol. Chem. 266, 8328-8335.
35. Matthews, B. W., Nicholson, H. & Becktel, W. J. (1987) Proc. Natl. Acad. Sci. USA 84, 6663-6667.
36. Russell, R. B. & Barton, G. J. (1992) Proteins Struct. Funct. Genet. 14, 309-323.
37. Barton, G. J. (1993) Protein Eng. 6, 37-40.
38. Kabsch, W. & Sander, C. (1983) Biopolymers 22, 2577-2637.
39. Esnouf, R. M. (1997) J. Mol. Graphics 10, 132-134.
40. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.
41. Meritt, E. A. & Murphy, M. E. P. (1994) Acta Crystallogr. D50, 869-873.
42. Esnouf, R. M. (1999) Acta Crystallogr. D55, 938-940
43. Morollo, A. A. & Eck, M. J. Nat. Struct. Biol. 8, 243-247.