Role of the Ω-loop in the activity, substrate specificity, and structure of class A β-lactamase

Biochemistry

Volumn 37, Issue 10, 1998, Pages 3286-3296

  Banerjee, Sooiay ^a   Pieper, Ursula ^a   Kapadia, Geeta ^a   Pannell, Lewis K ^b   Herzbere, Osnat ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CEPHALOSPORIN DERIVATIVE; PENICILLIN DERIVATIVE;

ACYLATION; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; MICHAELIS MENTEN KINETICS; NONHUMAN; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS; STEREOCHEMISTRY;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BASE SEQUENCE; BETA-LACTAMASES; BETA-LACTAMS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; ELECTROCHEMISTRY; KINETICS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE DELETION; STAPHYLOCOCCUS AUREUS; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS AUREUS;

EID: 0032502332     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972127f     Document Type: Article

References (47)

1. Ambler, R. P. (1980) Philos. Trans. R. Soc. London B289, 321-331.
2. Knott-Hunziker, V., Waley, S. G., Orlek, B. S., and Sammes, P. G. (1979) FEBS Lett. 99, 59-61.
3. Cartwright, S. J., and Coulson, A. F. W. (1980) Philos. Trans. R. Soc. London B289, 370-372.
4. Cohen, S. A., and Pratt, R. F. (1980) Biochemistry 19, 3996-4003.
5. Fisher, J., Belasco, J. G., Kohsla, S., and Knowles, J. R. (1980) Biochemistry 19, 2895-2901.
6. Ambler, R. P., Coulson, A. F. W, Frère, J.-M. Ghuysen, J.-M., Joris, B., Forsman, M., Levesque, R. C., Tiraby, G., and Waley, S. G. (1991) Biochem. J. 276, 269-270.
7. Herzberg, O., and Moult, J. (1987) Science 236, 694-701.
8. Herzberg, O. (1991) J. Mol. Biol. 217, 701-719.
9. Moews, P. C., Knox, J. R., Dideberg, O., Charlier, P., and Frère, J.-M. (1990) Proteins 7, 156-171.
10. Knox, J. R., and Moews, P. C. (1991) J. Mol. Biol. 220, 435-455.
11. Jelsch, C., Lenfant, F., Masson, J. M., and Samama, J. P. (1992) FEBS Lett. 299, 135-142.
12. Jelsch, C., Mourey, L. F., Masson, J. M., and Samama, J. P. (1993) Proteins 16, 364-383.
13. Strynadka, N. C. J., Adachi, H., Jensen, S. E., Johns, K., Sielecki, A., Betzel, C., Sutoh, K., and James, M. N. G. (1992) Nature 359, 700-705.
14. Herzberg, O., and Moult, J. (1991a) Curr. Opin. Struct. Biol. 1, 946-953.
15. Gibson, R. M., Christensen, H., and Waley, S. G. (1990) Biochem. J. 272, 613-619.
16. Oefner, C., D'Arcy, A., Daly, J. J., Gubernato, K., Chamas, R. L., Heinze, I., Hubschwerlen, C., and Winkler, F. K. (1990) Nature 343, 284-288.
17. Lobkovsky, E., Billing, E. M., Moews, P. C., Rahil, J., Pratt, R. F., and Knox, J. R. (1994) Biochemistry 33, 6762-6772.
18. Damblon, C., Raquet, X., Lian, L.-Y., Lamotte-Brasseur, J., Fonze, E., Charlier, P., Roberts, G. C. K., and Frère, J.-M. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 1747-1752.
19. Zawadzke, L. E., Chen, C. C. H., Banerjee, S., Li, Z., Wäsch, S., Kapadia, G., Moult, J., and Herzberg, O. (1996) Biochemists 35, 16475-16482.
20. Knox, J. R., Moews, P. C., and Frère, J.-M. (1996) Chem. Biol. 3, 937-947.
21. Herzberg, O., Kapadia, G., Blanco, B., Smith, T., and Coulson, A. F. W. (1991) Biochemistry 30, 9503-9509.
22. Adachi, H., Ohta, T., and Matsuzawa, H. (1991) J. Biol. Chem. 266, 3186-3191.
23. Escobar, W. A., Tan, A. K., and Fink, A. L. (1991) Biochemistry 30, 10783-10787.
24. Guillaume, G., Vanhove, M., Lamotte-Brasseur, J., Ledent, P., Jamin, M., Joris, B., and Frère, J.-M. (1997) J. Biol. Chem. 272, 5438-5444.
25. Banerjee, S., Shigematsu, N., Pannell, L. K., Ruvinov, S., Orban, J., Schwarz, F., and Herzberg, O. (1997) Biochemistry 36, 10857-10866.
26. Herzberg, O., and Moult, J. (1991b) Proteins: Struct., Funct., Genet. 11, 223-229.
27. Craig, S., Hollecker, M., Creighton, T. E., and Pain, R. H. (1985) J. Mol. Biol. 185, 681-687.
28. Zawadzke, L. E., Smith, T., and Herzberg, O (1995) Protein Eng. 8, 1275-1285.
29. Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Gene 77, 51-59.
30. Carrey, E. A., and Pain, R. H. (1978) Biochim. Biophys. Acta 533, 12-22.
31. Howard, A. J., Gilliland, G. L., Finzel, B. C., Poulos, T., Ohlendorf, D. O., and Salemme, F. R. (1987) J. Appl. Crystallogr. 20, 383-387.
32. Navaza, J. (1994) Acta Crystallogr. A50, 157-163.
33. Brünger, A. T. (1992a) X-PLOR version 3.1, a system for X-ray crystallography and NMR, Yale University Press, New Haven and London.
34. Brünger, A. T. (1992b) Nature 355, 472-475.
35. Roussel, A., and Cambillau, C. (1989) Silicon Graphics Directory, Silicon Graphics, Mountain View, CA.
36. Satow, Y., Cohen, G. H., Padlan, E. A., and Davies, D. R. (1986) J. Mol. Biol. 190, 593-604.
37. Sweet, R. M., and Dahl, L. F. (1970) J. Am. Chem. Soc. 92, 5489-5495.
38. Engh, R. A., and Huber, R. (1991) Acta Crystallogr. A47, 392-400.
39. Chen, C. C. H., and Herzberg, O. (1991) J. Mol. Biol. 224, 1103-1113.
40. Chen, C. C. H., Rahil, J., Pratt, R. F., and Herzberg, O. (1992) J. Mol. Biol. 234, 165-178.
41. Waley, S. G. (1991) Biochem. J. 279, 87-94.
42. Mitchinson, C., and Pain, R. H. (1985) J. Mol. Biol. 184, 331-342.
43. Escobar, W. A., Tan, A. K., Lewis, E. R., and Fink, A. L. (1994) Biochemistry 33, 7619-7626.
44. Faraci, W. S., and Pratt, R. F. (1985) Biochemistry 24, 903-910.
45. Galleni, M., and Frère, J.-M. (1988) Biochem. J. 255, 119-122.
46. Matagne, A., Misselyn-Bauduin, A.-M., Joris, B., Erpicum, T., Granier, B., and Frère, J.-M. (1990) Biochem J. 265, 131-146.
47. Lobkovsky, E., Moews, P. C., Liu, H., Zhao, H., Frère, J.-M., and Knox, J. R. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 11257-11261.