4V64
Crystal structure of the bacterial ribosome from Escherichia coli in complex with hygromycin B.
This is a non-PDB format compatible entry.
Summary for 4V64
| Entry DOI | 10.2210/pdb4v64/pdb |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (56 entities in total) |
| Functional Keywords | rna-protein complex, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 104 |
| Total formula weight | 4296888.47 |
| Authors | Borovinskaya, M.A.,Shoji, S.,Fredrick, K.,Cate, J.H.D. (deposition date: 2008-06-11, release date: 2014-07-09, Last modification date: 2023-09-20) |
| Primary citation | Borovinskaya, M.A.,Shoji, S.,Fredrick, K.,Cate, J.H.D. Structural basis for hygromycin B inhibition of protein biosynthesis Rna, 14:1590-1599, 2008 Cited by PubMed Abstract: Aminoglycosides are one of the most widely used and clinically important classes of antibiotics that target the ribosome. Hygromycin B is an atypical aminoglycoside antibiotic with unique structural and functional properties. Here we describe the structure of the intact Escherichia coli 70S ribosome in complex with hygromycin B. The antibiotic binds to the mRNA decoding center in the small (30S) ribosomal subunit of the 70S ribosome and induces a localized conformational change, in contrast to its effects observed in the structure of the isolated 30S ribosomal subunit in complex with the drug. The conformational change in the ribosome caused by hygromycin B binding differs from that induced by other aminoglycosides. Also, in contrast to other aminoglycosides, hygromycin B potently inhibits spontaneous reverse translocation of tRNAs and mRNA on the ribosome in vitro. These structural and biochemical results help to explain the unique mode of translation inhibition by hygromycin B. PubMed: 18567815DOI: 10.1261/rna.1076908 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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