6W6P
MultiBody Refinement of 70S Ribosome from Enterococcus faecalis
This is a non-PDB format compatible entry.
Summary for 6W6P
| Entry DOI | 10.2210/pdb6w6p/pdb |
| EMDB information | 0656 0657 0658 0659 0660 21562 |
| Descriptor | 16S rRNA, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (48 entities in total) |
| Functional Keywords | 70s, ribosome, pathogen, antibiotic development, antibiotic resistant |
| Biological source | Enterococcus faecalis OG1RF More |
| Total number of polymer chains | 47 |
| Total formula weight | 2046927.51 |
| Authors | Jogl, G.,Khayat, R. (deposition date: 2020-03-17, release date: 2020-10-14, Last modification date: 2024-03-06) |
| Primary citation | Murphy, E.L.,Singh, K.V.,Avila, B.,Kleffmann, T.,Gregory, S.T.,Murray, B.E.,Krause, K.L.,Khayat, R.,Jogl, G. Cryo-electron microscopy structure of the 70S ribosome from Enterococcus faecalis. Sci Rep, 10:16301-16301, 2020 Cited by PubMed Abstract: Enterococcus faecalis is a gram-positive organism responsible for serious infections in humans, but as with many bacterial pathogens, resistance has rendered a number of commonly used antibiotics ineffective. Here, we report the cryo-EM structure of the E. faecalis 70S ribosome to a global resolution of 2.8 Å. Structural differences are clustered in peripheral and solvent exposed regions when compared with Escherichia coli, whereas functional centres, including antibiotic binding sites, are similar to other bacterial ribosomes. Comparison of intersubunit conformations among five classes obtained after three-dimensional classification identifies several rotated states. Large ribosomal subunit protein bL31, which forms intersubunit bridges to the small ribosomal subunit, assumes different conformations in the five classes, revealing how contacts to the small subunit are maintained throughout intersubunit rotation. A tRNA observed in one of the five classes is positioned in a chimeric pe/E position in a rotated ribosomal state. The 70S ribosome structure of E. faecalis now extends our knowledge of bacterial ribosome structures and may serve as a basis for the development of novel antibiotic compounds effective against this pathogen. PubMed: 33004869DOI: 10.1038/s41598-020-73199-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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