Aminoglycoside antibiotics bound to aminoglycoside-detoxifying enzymes and RNA adopt similar conformations

Cell Biochemistry and Biophysics

Volumn 33, Issue 3, 2000, Pages 297-308

  Cox, James R ^a   Ekman, Drew R ^b   DiGiammarino, Enrico L ^c   Akal Strader, Ayça ^b   Serpersu, Engin H ^b  

^a MURRAY STATE UNIVERSITY   (United States)

^b ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

^c UNIVERSITY OF TENNESSEE   (United States)

Author keywords

Aminoglycoside detoxification; Aminoglycosides; Antibiotic resistance; Antibiotic structure; Antibiotics; Isepamicin; Nuclear magnetic resonance (NMR); Ribostamycin; Substrate conformation

Indexed keywords

KANAMYCIN; KANAMYCIN KINASE; RIBOSOME RNA; RIBOSTAMYCIN;

ANIMAL; ARTICLE; CHEMISTRY; CONFORMATION; ENZYME SPECIFICITY; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION;

ANIMALS; KANAMYCIN; KANAMYCIN KINASE; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN CONFORMATION; RIBOSTAMYCIN; RNA, RIBOSOMAL; SUBSTRATE SPECIFICITY;

EID: 0034577239     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:33:3:297     Document Type: Article

References (22)

1. Umezawa, H. (1974) Biochemical mechanism of resistance to aminoglycoside antibiotics, in Advances in Carbohydrate Chemistry and Biochemistry (Tipson, R. S. and Horton, D., eds.), vol. 30, Academic, New York, pp. 183-225.
2. Cox, J. R., McKay, G. A., Wright, G. D., and Serpersu, E. H. (1996) Arrangement of substrates at the active site of an aminoglycoside antibiotic 3'-phosphotransferase. J. Am. Chem. Soc. 118, 1295-1301.
3. Cox, J. R. and Serpersu, E. H. (1997) Biologically important conformations of aminoglycoside antibiotics bound to an aminoglycoside 3′-phosphotransferase as determined by transferred nuclear Overhauser effect spectroscopy. Biochemistry 36, 2353-2359.
4. Mohler, L. M., Cox, J. R., and Serpersu, E. H. (1998) Aminoglycoside phosphotransferase(3′)-IIIa (APH(3′)-IIIa)-bound conformation of the aminoglycoside lividomycin A characterized by NMR. Carbohydr. Lett. 3, 17-24.
5. Davies, J. (1994) Inactivation of antibiotics and the dissemination of resistance genes. Science 264, 375-382.
6. Shaw, K. J., Rather, P. N., Hare, R. S., Miller, G. H. (1993) Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes. Microbiol. Rev. 57, 138-163.
7. Moellering, R. C. (1991) The Garrod lecture. The Enterococcus: a classical example of the impact of antimicrobial resistance on therapeutic options. J. Antimicrob. Chemother. 28, 1-12.
8. Spera, R. V. and Farber, B. F. (1992) Multiply-resistant Enterococcus faecium: the nosocomial pathogen of 1990s. JAMA 268, 2563-2564.
9. Zembower, T. R., Noskin, G. A., Postelnick, M. J., Nguyen, C., and Peterson, E. R. (1998) The utility of aminoglycosides in an era of emerging drug resistance. Int. J. Antimicrob. Agents 10, 95-105.
10. McKay, G. A., Thompson, P. R., and Wright, G. D. (1994) Broad spectrum aminoglycoside phosphotransferase type III from enterococcus: overexpression, purification and substrate specificity. Biochemistry 33, 6936-6944.
11. Cox, J. R. and Serpersu, E. H. (1995) The complete proton assignments of aminoglycoside antibiotics and conformational studies of butirosin through the use of 2D NMR. Carbohydr. Res. 271, 55-63.
12. 15N nuclear magnetic resonance study. Magn. Reson. Chem. 30, 11.
13. Clore, G. M. and Gronenborn, A. M. (1982) Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins J. Magn. Res. 48, 402-417.
14. Neuhaus, D. and Williamson, M. P. (1989) The Nuclear Overhauser Effect in Structural and Conformational Analysis. VCH, New York.
15. Shaka, A. J., Keeler, J., and Freeman, R. (1983) Evaluation of a new broad band decoupling sequence: WALTZ-16. J. Magn. Reson. 53, 313-340.
16. Weiner, S. J., Kollman, P. A., Nguyen, D. T., and Case, D. A. (1986) An all atom force field for simulations of proteins and nucleic acids. J. Comput. Chem. 7, 230.
17. Homans, S. W. (1990) A molecular mechanical force field for the conformational analysis of oligosaccharides: comparison of theoretical and crystal structures of Manα1-3Manβ1-4GlcNAc. Biochemistry 29, 9110-9118.
18. DiGiammarino, E. L., Draker, K., Wright, G. D., and Serpersu, E. H. (1998) Solution studies of isepamicin and conformational comparisons between isepamicin and butirosin A when bound to an aminoglycoside 6′-N-acetyltransferase determined by NMR spectroscopy. Biochemistry 37, 3638-3644.
19. Homans, S. W. and Forster, M. (1992) Application of restrained minimization, simulated annealing and molecular dynamics simulations for the conformational analysis of oligosaccharides. Glycobiology 2, 143-151.
20. Fourmy, D., Recht, M. I., Blanchard, S. C., and Puglisi, J. D. (1996) Structure of the A site of Esherichia coli 16s ribosomal RNA complexed with an aminoglycoside antibiotic. Science 274, 1367-1371.
21. Jiang, L., Suri, A. K., Fiala, R., and Patel, D. J. (1997) Saccharide-RNA recognition in an aminoglycoside antibiotic-RNA aptamer complex. Chem. Biol. 4, 35.
22. Yoshizawa, S., Fourmy, D., and Puglisi, J. (1998) Structural origins of gentamycin antibiotic action. EMBO J. 17, 6437-6448.