4U1V
Crystal structure of the E. coli ribosome bound to linopristin.
This is a non-PDB format compatible entry.
Summary for 4U1V
| Entry DOI | 10.2210/pdb4u1v/pdb |
| Related PRD ID | PRD_002101 |
| Descriptor | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (57 entities in total) |
| Functional Keywords | protein biosynthesis, ribosome, rna, transfer, exit, peptidyl, 30s, 70s, 16s, ribosomal subunit, antibiotic, streptogramin |
| Biological source | Escherichia coli str. K-12 substr. MDS42 More |
| Total number of polymer chains | 107 |
| Total formula weight | 4269799.34 |
| Authors | Noeske, J.,Huang, J.,Olivier, N.B.,Giacobbe, R.A.,Zambrowski, M.,Cate, J.H.D. (deposition date: 2014-07-16, release date: 2014-07-30, Last modification date: 2024-10-16) |
| Primary citation | Noeske, J.,Huang, J.,Olivier, N.B.,Giacobbe, R.A.,Zambrowski, M.,Cate, J.H. Synergy of streptogramin antibiotics occurs independently of their effects on translation. Antimicrob.Agents Chemother., 58:5269-5279, 2014 Cited by PubMed Abstract: Streptogramin antibiotics are divided into types A and B, which in combination can act synergistically. We compared the molecular interactions of the streptogramin combinations Synercid (type A, dalfopristin; type B, quinupristin) and NXL 103 (type A, flopristin; type B, linopristin) with the Escherichia coli 70S ribosome by X-ray crystallography. We further analyzed the activity of the streptogramin components individually and in combination. The streptogramin A and B components in Synercid and NXL 103 exhibit synergistic antimicrobial activity against certain pathogenic bacteria. However, in transcription-coupled translation assays, only combinations that include dalfopristin, the streptogramin A component of Synercid, show synergy. Notably, the diethylaminoethylsulfonyl group in dalfopristin reduces its activity but is the basis for synergy in transcription-coupled translation assays before its rapid hydrolysis from the depsipeptide core. Replacement of the diethylaminoethylsulfonyl group in dalfopristin by a nonhydrolyzable group may therefore be beneficial for synergy. The absence of general streptogramin synergy in transcription-coupled translation assays suggests that the synergistic antimicrobial activity of streptogramins can occur independently of the effects of streptogramin on translation. PubMed: 24957822DOI: 10.1128/AAC.03389-14 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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