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4KHP

Structure of the Thermus thermophilus 30S ribosomal subunit in complex with de-6-MSA-pactamycin

Summary for 4KHP
Entry DOI10.2210/pdb4khp/pdb
Related1HNX
Descriptor16S Ribosomal RNA, 30S Ribosomal protein S10, 30S Ribosomal protein S11, ... (25 entities in total)
Functional Keywordspactamycin, 30s, mrna, e site, trna, ribosome, translation, antibiotic, ribosome-antibiotic complex, de-6-msa-pactamycin and pactamycin analog, ribosome/antibiotic
Biological sourceThermus thermophilus
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Total number of polymer chains22
Total formula weight770160.41
Authors
Tourigny, D.S.,Fernandez, I.S.,Kelley, A.C.,Ramakrishnan, V. (deposition date: 2013-05-01, release date: 2013-06-05, Last modification date: 2024-11-06)
Primary citationTourigny, D.S.,Fernandez, I.S.,Kelley, A.C.,Vakiti, R.R.,Chattopadhyay, A.K.,Dorich, S.,Hanessian, S.,Ramakrishnan, V.
Crystal Structure of a Bioactive Pactamycin Analog Bound to the 30S Ribosomal Subunit.
J.Mol.Biol., 425:3907-3910, 2013
Cited by
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-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.
PubMed: 23702293
DOI: 10.1016/j.jmb.2013.05.004
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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