4khp: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/RSHX_THET8 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. | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23702293</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4khp" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Ribosomal protein THX 3D structures|Ribosomal protein THX 3D structures]] | *[[Ribosomal protein THX 3D structures|Ribosomal protein THX 3D structures]] | ||
*[[Ribosome 3D structures|Ribosome 3D structures]] | *[[Ribosome 3D structures|Ribosome 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 14:03, 6 November 2024
Structure of the Thermus thermophilus 30S ribosomal subunit in complex with de-6-MSA-pactamycinStructure of the Thermus thermophilus 30S ribosomal subunit in complex with de-6-MSA-pactamycin
Structural highlights
FunctionRSHX_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 PubMedBiosynthetically 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 AlsoReferences
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