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The L7/12 stalk of the large subunit of bacterial ribosomes encompasses protein L10 and multiple copies of L7/12. We present crystal structures of Thermotoga maritima L10 in complex with three L7/12 N-terminal-domain dimers, refine the structure of an archaeal L10E N-terminal domain on the 50S subunit, and identify these elements in(More)
Ribosomes, the site of protein synthesis, are a major target for natural and synthetic antibiotics. Detailed knowledge of antibiotic binding sites is central to understanding the mechanisms of drug action. Conversely, drugs are excellent tools for studying the ribosome function. To elucidate the structural basis of ribosome-antibiotic interactions, we(More)
Despite the appearance of bacterial strains resistant to all clinical antibiotics, including vancomycin (the 'last resort'), development of new antimicrobial agents has slowed during recent decades. To aid design of new antibiotics, we must develop a detailed understanding of the mechanisms of antibiotic action and antibiotic resistance. Several classes of(More)
BACKGROUND The bacterial ribosome is a primary target of several classes of antibiotics. Investigation of the structure of the ribosomal subunits in complex with different antibiotics can reveal the mode of inhibition of ribosomal protein synthesis. Analysis of the interactions between antibiotics and the ribosome permits investigation of the specific(More)
Elongation (translocation) Most aminoglycoside antibiotics induce translational misreading by promoting binding of near-cognate tRNAs, but the biological effect is probably due to inhibition of the translocation reaction and promotion of back-translocation. Edeine Edeine A Initiation (fMet-tRNA binding) Edeine prevents binding of the initiator tRNA to the(More)
The translational apparatus is one of the major targets for antibiotics in the bacterial cell. Antibiotics predominantly interact with the functional centers of the ribosome, namely the messenger RNA (mRNA)-transfer RNA (tRNA) decoding region on the 30S subunit, the peptidyltransferase center on the 50S subunit, or the ribosomal exit tunnel through which(More)
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