Structural highlights
Function
RSHX_THET8 Binds at the top of the head of the 30S subunit. It stabilizes a number of different RNA elements and thus is important for subunit structure.
Publication Abstract from PubMed
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-A 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.
Crystal Structure of a Bioactive Pactamycin Analog Bound to the 30S Ribosomal Subunit.,Tourigny DS, Fernandez IS, Kelley AC, Vakiti RR, Chattopadhyay AK, Dorich S, Hanessian S, Ramakrishnan V J Mol Biol. 2013 May 20. pii: S0022-2836(13)00303-3. doi:, 10.1016/j.jmb.2013.05.004. PMID:23702293[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tourigny DS, Fernandez IS, Kelley AC, Vakiti RR, Chattopadhyay AK, Dorich S, Hanessian S, Ramakrishnan V. Crystal Structure of a Bioactive Pactamycin Analog Bound to the 30S Ribosomal Subunit. J Mol Biol. 2013 May 20. pii: S0022-2836(13)00303-3. doi:, 10.1016/j.jmb.2013.05.004. PMID:23702293 doi:10.1016/j.jmb.2013.05.004
