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6WUB

30S subunit (head) of 70S Ribosome Enterococcus faecalis MultiBody refinement

Summary for 6WUB
Entry DOI10.2210/pdb6wub/pdb
EMDB information0656 0657 0658 0659 0660 21909
Descriptor16S rRNA, 30S ribosomal protein S17, 30S ribosomal protein S18, ... (12 entities in total)
Functional Keywords70s, ribosome, pathogen, antibiotic development, antibiotic resistant
Biological sourceEnterococcus faecalis OG1RF
More
Total number of polymer chains12
Total formula weight641780.11
Authors
Jogl, G.,Khayat, R. (deposition date: 2020-05-04, release date: 2020-11-04, Last modification date: 2024-03-06)
Primary citationMurphy, 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: 33004869
DOI: 10.1038/s41598-020-73199-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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