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Crystal Structure of a Bioactive Pactamycin Analog Bound to the 30S Ribosomal Subunit
- Tourigny, David S., Fernández, Israel S., Kelley, Ann C., Vakiti, Ramkrishna Reddy, Chattopadhyay, Amit Kumar, Dorich, Stéphane, Hanessian, Stephen, Ramakrishnan, V.
- Journal of Molecular Biology 2013 v.425 pp. 3907-3910
- Thermus thermophilus, antibiotics, antineoplastic agents, binding sites, crystal structure, nucleic acids, ribosomes
- Biosynthetically and chemically derived analogs of the antibiotic pactamycin and de-6-methylsalicylyl (MSA)-pactamycin have attracted recent interest as potential antiprotozoal and antitumor drugs. Here, we report a 3.1-Å crystal structure of de-6-MSA-pactamycin bound to its target site on the Thermus thermophilus 30S ribosomal subunit. Although de-6-MSA-pactamycin lacks the MSA moiety, it shares the same binding site as pactamycin and induces a displacement of nucleic acid template bound at the E-site of the 30S. The structure highlights unique interactions between this pactamycin analog and the ribosome, which paves the way for therapeutic development of related compounds.