Structural insight into the antibiotic action of telithromycin against resistant mutants (203 visite)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Tipo di articolo: Journal Article,
Impact factor: 4.175, Impact factor a 5 anni: 3.298
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0038492422&partnerID=40&md5=46b4241b4cf7905242d3a5efe211743f
Parole chiave: Cethromycin, Erythromycin, Ketolide, Macrolide, Telithromycin, Antibiotic Resistance, Article, Bacterium Mutant, Binding Site, Crystal Structure, Deinococcus Radiodurans, Drug Mechanism, Drug Protein Binding, Drug Structure, Nonhuman, Priority Journal, Protein Domain, Protein Interaction, Ribosome, Anti-Bacterial Agents, Crystallization, Crystallography, X-Ray, Drug Resistance, Models, Molecular, Molecular Sequence Data, 23s, Bacteria (microorganisms), Posibacteria,
Affiliazioni:
*** IBB - CNR ***
Max-Planck-Res. U. Ribosomal Struct., Hamburg, Germany
Max-Planck-Inst. for Molec. Genet., Berlin, Germany
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Inst. of Biostructure and Bioimaging, CNR, Naples, Italy
Riferimenti:
Abrahams, J.P., Leslie, A.G.W., Methods used in the structure determination of bovine mitochondrial F-1 ATPase (1996) Acta Crystallogr. D, 52, pp. 30-4
Bailey, S., The CCP4 suite - Programs for protein crystallography (1994) Acta Crystallogr. D, 50, pp. 760-763
Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., Yonath, A., Structural insight into the role of the ribosomal tunnel in cellular regulation (2003) Nat. Struct. Biol., 10, pp. 366-370
Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Warren, G.L., Crystallography & NMR System: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. D, 54, pp. 905-921
Carson, M., Ribbons (1997) Macromol. Crystallogr. B, 277, pp. 493-505
Douthwaite, S., Hansen, L.H., Mauvais, P., Macrolide-ketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA (2000) Mol. Microbiol., 36, pp. 183-193
Goldman, R.C., Fesik, S.W., Doran, C.C., Role of protonated and neutral forms of macrolides in binding to ribosomes from gram-positive and gram-negative bacteria (1990) Antimicrob. Agents Chemother., 34, pp. 426-431
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., High resolution structure of the large ribosomal subunit from a mesophilic eubacterium (2001) Cell, 107, pp. 679-688
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47 (PART 2), pp. 110-119
Liu, M., Douthwaite, S., Activity of the ketolide telithromycin is refractory to Erm monomethylation of bacterial rRNA (2002) Antimicrob. Agents Chemother., 46, pp. 1629-1633
Okamoto, H., Miyazaki, S., Tateda, K., Ishii, Y., Yamaguchi, K., In vivo efficacy of telithromycin (HMR3647) against Streptococcus pneumoniae and Haemophilus influenzae (2001) Antimicrob. Agents Chemother., 45, pp. 3250-3252
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Macromol. Crystallogr. A, 276, pp. 307-326
Shain, C.S., Amsden, G.W., Telithromycin: The first of the ketolides (2002) Ann. Pharmacother., 36, pp. 452-464
Wallace, A.C., Laskowski, R.A., Thornton, J.M., LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions (1995) Protein Eng., 8, pp. 127-134
Weisblum, B., Erythromycin resistance by ribosome modification (1995) Antimicrob. Agents Chemother., 39, pp. 577-585
Xiong, L., Kloss, P., Douthwaite, S., Andersen, N.M., Swaney, S., Shinabarger, D.L., Mankin, A.S., Oxazolidinone resistance mutations in 23S rRNA of Escherichia coli reveal the central region of domain V as the primary site of drug action (2000) J. Bacteriol., 182, pp. 5325-5331
Xiong, L., Shah, S., Mauvais, P., Mankin, A.S., A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre (1999) Mol. Microbiol., 31, pp. 633-639
Abrahams, J. P., Leslie, A. G. W., Methods used in the structure determination of bovine mitochondrial F-1 ATPase (1996) Acta Crystallogr. D, 52, pp. 30-4
Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Warren, G. L., Crystallography & NMR System: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. D, 54, pp. 905-921
Goldman, R. C., Fesik, S. W., Doran, C. C., Role of protonated and neutral forms of macrolides in binding to ribosomes from gram-positive and gram-negative bacteria (1990) Antimicrob. Agents Chemother., 34, pp. 426-431
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47 (PART 2), pp. 110-119
Shain, C. S., Amsden, G. W., Telithromycin: The first of the ketolides (2002) Ann. Pharmacother., 36, pp. 452-464
Wallace, A. C., Laskowski, R. A., Thornton, J. M., LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions (1995) Protein Eng., 8, pp. 127-134
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Tipo di articolo: Journal Article,
Impact factor: 4.175, Impact factor a 5 anni: 3.298
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0038492422&partnerID=40&md5=46b4241b4cf7905242d3a5efe211743f
Parole chiave: Cethromycin, Erythromycin, Ketolide, Macrolide, Telithromycin, Antibiotic Resistance, Article, Bacterium Mutant, Binding Site, Crystal Structure, Deinococcus Radiodurans, Drug Mechanism, Drug Protein Binding, Drug Structure, Nonhuman, Priority Journal, Protein Domain, Protein Interaction, Ribosome, Anti-Bacterial Agents, Crystallization, Crystallography, X-Ray, Drug Resistance, Models, Molecular, Molecular Sequence Data, 23s, Bacteria (microorganisms), Posibacteria,
Affiliazioni:
*** IBB - CNR ***
Max-Planck-Res. U. Ribosomal Struct., Hamburg, Germany
Max-Planck-Inst. for Molec. Genet., Berlin, Germany
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Inst. of Biostructure and Bioimaging, CNR, Naples, Italy
Riferimenti:
Abrahams, J.P., Leslie, A.G.W., Methods used in the structure determination of bovine mitochondrial F-1 ATPase (1996) Acta Crystallogr. D, 52, pp. 30-4
Bailey, S., The CCP4 suite - Programs for protein crystallography (1994) Acta Crystallogr. D, 50, pp. 760-763
Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., Yonath, A., Structural insight into the role of the ribosomal tunnel in cellular regulation (2003) Nat. Struct. Biol., 10, pp. 366-370
Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Warren, G.L., Crystallography & NMR System: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. D, 54, pp. 905-921
Carson, M., Ribbons (1997) Macromol. Crystallogr. B, 277, pp. 493-505
Douthwaite, S., Hansen, L.H., Mauvais, P., Macrolide-ketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA (2000) Mol. Microbiol., 36, pp. 183-193
Goldman, R.C., Fesik, S.W., Doran, C.C., Role of protonated and neutral forms of macrolides in binding to ribosomes from gram-positive and gram-negative bacteria (1990) Antimicrob. Agents Chemother., 34, pp. 426-431
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., High resolution structure of the large ribosomal subunit from a mesophilic eubacterium (2001) Cell, 107, pp. 679-688
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47 (PART 2), pp. 110-119
Liu, M., Douthwaite, S., Activity of the ketolide telithromycin is refractory to Erm monomethylation of bacterial rRNA (2002) Antimicrob. Agents Chemother., 46, pp. 1629-1633
Okamoto, H., Miyazaki, S., Tateda, K., Ishii, Y., Yamaguchi, K., In vivo efficacy of telithromycin (HMR3647) against Streptococcus pneumoniae and Haemophilus influenzae (2001) Antimicrob. Agents Chemother., 45, pp. 3250-3252
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Macromol. Crystallogr. A, 276, pp. 307-326
Shain, C.S., Amsden, G.W., Telithromycin: The first of the ketolides (2002) Ann. Pharmacother., 36, pp. 452-464
Wallace, A.C., Laskowski, R.A., Thornton, J.M., LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions (1995) Protein Eng., 8, pp. 127-134
Weisblum, B., Erythromycin resistance by ribosome modification (1995) Antimicrob. Agents Chemother., 39, pp. 577-585
Xiong, L., Kloss, P., Douthwaite, S., Andersen, N.M., Swaney, S., Shinabarger, D.L., Mankin, A.S., Oxazolidinone resistance mutations in 23S rRNA of Escherichia coli reveal the central region of domain V as the primary site of drug action (2000) J. Bacteriol., 182, pp. 5325-5331
Xiong, L., Shah, S., Mauvais, P., Mankin, A.S., A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre (1999) Mol. Microbiol., 31, pp. 633-639
Abrahams, J. P., Leslie, A. G. W., Methods used in the structure determination of bovine mitochondrial F-1 ATPase (1996) Acta Crystallogr. D, 52, pp. 30-4
Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Warren, G. L., Crystallography & NMR System: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. D, 54, pp. 905-921
Goldman, R. C., Fesik, S. W., Doran, C. C., Role of protonated and neutral forms of macrolides in binding to ribosomes from gram-positive and gram-negative bacteria (1990) Antimicrob. Agents Chemother., 34, pp. 426-431
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47 (PART 2), pp. 110-119
Shain, C. S., Amsden, G. W., Telithromycin: The first of the ketolides (2002) Ann. Pharmacother., 36, pp. 452-464
Wallace, A. C., Laskowski, R. A., Thornton, J. M., LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions (1995) Protein Eng., 8, pp. 127-134
The crystal structure of the ketolide telithromycin bound to the Deinococcus radiodurans large ribosomal subunit shows that telithromycin blocks the ribosomal exit tunnel and interacts with domains II and V of the 23S RNA. Comparisons to other clinically relevant macrolides provided structural insights into its enhanced activity against macrolide-resistant strains.
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