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4V7L

The structures of viomycin bound to the 70S ribosome.

This is a non-PDB format compatible entry.
Summary for 4V7L
Entry DOI10.2210/pdb4v7l/pdb
Related3KNL 3KNM 3KNN 3KNO
Related PRD IDPRD_000226
Descriptor16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (60 entities in total)
Functional Keywordsanti-tuberculosis antibiotic, 70s, ribosome, trna, mrna, tuberactinomycin, viomycin, ribosome-antibiotic complex, ribosome/antibiotic
Biological sourceEscherichia coli
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Total number of polymer chains116
Total formula weight4569802.28
Authors
Stanley, R.E.,Blaha, G. (deposition date: 2009-11-12, release date: 2014-07-09, Last modification date: 2018-07-11)
Primary citationStanley, R.E.,Blaha, G.,Grodzicki, R.L.,Strickler, M.D.,Steitz, T.A.
The structures of the anti-tuberculosis antibiotics viomycin and capreomycin bound to the 70S ribosome.
Nat.Struct.Mol.Biol., 17:289-293, 2010
Cited by
PubMed Abstract: Viomycin and capreomycin belong to the tuberactinomycin family of antibiotics, which are among the most effective antibiotics against multidrug-resistant tuberculosis. Here we present two crystal structures of the 70S ribosome in complex with three tRNAs and bound to either viomycin or capreomycin at 3.3- and 3.5-A resolution, respectively. Both antibiotics bind to the same site on the ribosome, which lies at the interface between helix 44 of the small ribosomal subunit and helix 69 of the large ribosomal subunit. The structures of these complexes suggest that the tuberactinomycins inhibit translocation by stabilizing the tRNA in the A site in the pretranslocation state. In addition, these structures show that the tuberactinomycins bind adjacent to the binding sites for the paromomycin and hygromycin B antibiotics, which may enable the development of new derivatives of tuberactinomycins that are effective against drug-resistant strains.
PubMed: 20154709
DOI: 10.1038/nsmb.1755
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

229380

數據於2024-12-25公開中

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