Oxazolidinone Antibiotics Target the P Site on Escherichia coli Ribosomes
نویسندگان
چکیده
منابع مشابه
Oxazolidinone antibiotics target the P site on Escherichia coli ribosomes.
The oxazolidinones are a novel class of antimicrobial agents that target protein synthesis in a wide spectrum of gram-positive and anaerobic bacteria. The oxazolidinone PNU-100766 (linezolid) inhibits the binding of fMet-tRNA to 70S ribosomes. Mutations to oxazolidinone resistance in Halobacterium halobium, Staphylococcus aureus, and Escherichia coli map at or near domain V of the 23S rRNA, sug...
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Erythromycin binding to Escherichia coli ribosomes required K+ and Mg2+. Under optimal conditions, the dissociation constant for erythromycin binding to E. coli ribosomes was found to be 1.0 x 108M and 1.4 x 108M at 24 C and 5 C, respectively. One molecule of [I4C Jerythromycin was bound to each 70S ribosome at equilibrium. Binding of erythromycin to ribosomes was rapid and reversible. The spec...
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The knowledge of the structure of the ribosome is an essential requirement to reveal its role at the molecular level in the process of protein biosynthesis. This information is being obtained by a battery of chemical, physical, immunological and genetic methods (for reviews see [1]). Important methods for the study of the three-dimensional structure of the ribosomes are X-ray crystallography an...
متن کاملImpact of P-Site tRNA and Antibiotics on Ribosome Mediated Protein Folding: Studies Using the Escherichia coli Ribosome
BACKGROUND The ribosome, which acts as a platform for mRNA encoded polypeptide synthesis, is also capable of assisting in folding of polypeptide chains. The peptidyl transferase center (PTC) that catalyzes peptide bond formation resides in the domain V of the 23S rRNA of the bacterial ribosome. Proper positioning of the 3' -CCA ends of the A- and P-site tRNAs via specific interactions with the ...
متن کاملtRNA binding sites on the subunits of Escherichia coli ribosomes.
Programmed 30 S subunits expose only one binding site, to which the different classes of tRNA (deacylated tRNAPhe, Phe-tRNAPhe, and N-acetylphenylalanyl (AcPhe)-tRNAPhe) bind with about the same affinity. Elongation factor Tu within the ternary complex does not contribute to the binding of Phe-tRNA. Binding of acylated or deacylated tRNA to 30 S depends on the cognate codon; nonprogrammed 30 S ...
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ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 2002
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.46.4.1080-1085.2002