4V4H
Crystal structure of the bacterial ribosome from Escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution.
This is a non-PDB format compatible entry.
Summary for 4V4H
| Entry DOI | 10.2210/pdb4v4h/pdb |
| Related | 1VS6 1VS7 1VS8 |
| Descriptor | 16S RIBOSOMAL RNA, 30S RIBOSOMAL PROTEIN S11, 30S RIBOSOMAL PROTEIN S12, ... (55 entities in total) |
| Functional Keywords | ribosome, kasugamycin |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 104 |
| Total formula weight | 4301002.66 |
| Authors | Schuwirth, B.S.,Vila-Sanjurjo, A.,Cate, J.H.D. (deposition date: 2006-08-04, release date: 2014-07-09, Last modification date: 2023-09-20) |
| Primary citation | Schuwirth, B.S.,Day, J.M.,Hau, C.W.,Janssen, G.R.,Dahlberg, A.E.,Cate, J.H.D.,Vila-Sanjurjo, A. Structural analysis of kasugamycin inhibition of translation. Nat.Struct.Mol.Biol., 13:879-886, 2006 Cited by PubMed Abstract: The prokaryotic ribosome is an important target of antibiotic action. We determined the X-ray structure of the aminoglycoside kasugamycin (Ksg) in complex with the Escherichia coli 70S ribosome at 3.5-A resolution. The structure reveals that the drug binds within the messenger RNA channel of the 30S subunit between the universally conserved G926 and A794 nucleotides in 16S ribosomal RNA, which are sites of Ksg resistance. To our surprise, Ksg resistance mutations do not inhibit binding of the drug to the ribosome. The present structural and biochemical results indicate that inhibition by Ksg and Ksg resistance are closely linked to the structure of the mRNA at the junction of the peptidyl-tRNA and exit-tRNA sites (P and E sites). PubMed: 16998486DOI: 10.1038/nsmb1150 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.46 Å) |
Structure validation
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