4KHP
Structure of the Thermus thermophilus 30S ribosomal subunit in complex with de-6-MSA-pactamycin
Summary for 4KHP
Entry DOI | 10.2210/pdb4khp/pdb |
Related | 1HNX |
Descriptor | 16S Ribosomal RNA, 30S Ribosomal protein S10, 30S Ribosomal protein S11, ... (25 entities in total) |
Functional Keywords | pactamycin, 30s, mrna, e site, trna, ribosome, translation, antibiotic, ribosome-antibiotic complex, de-6-msa-pactamycin and pactamycin analog, ribosome/antibiotic |
Biological source | Thermus thermophilus More |
Total number of polymer chains | 22 |
Total formula weight | 770160.41 |
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 citation | Tourigny, 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: 23702293DOI: 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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