Crystal Structure of a Bioactive Pactamycin Analog Bound to the 30S Ribosomal Subunit.
Tourigny, D.S., Fernandez, I.S., Kelley, A.C., Vakiti, R.R., Chattopadhyay, A.K., Dorich, S., Hanessian, S., Ramakrishnan, V.(2013) J Mol Biol 425: 3907-3910
- PubMed: 23702293 
- DOI: https://doi.org/10.1016/j.jmb.2013.05.004
- Primary Citation of Related Structures:  
4KHP - PubMed Abstract: 
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-? 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.
Organizational Affiliation: 
Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.