Summary for 6PJ6
| Entry DOI | 10.2210/pdb6pj6/pdb |
| EMDB information | 20353 |
| Descriptor | 23S rRNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (35 entities in total) |
| Functional Keywords | ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 31 |
| Total formula weight | 1356032.38 |
| Authors | Stojkovic, V.,Myasnikov, A.,Frost, A.,Fujimori, D.G. (deposition date: 2019-06-27, release date: 2020-01-22, Last modification date: 2023-11-15) |
| Primary citation | Stojkovic, V.,Myasnikov, A.G.,Young, I.D.,Frost, A.,Fraser, J.S.,Fujimori, D.G. Assessment of the nucleotide modifications in the high-resolution cryo-electron microscopy structure of the Escherichia coli 50S subunit. Nucleic Acids Res., 48:2723-2732, 2020 Cited by PubMed Abstract: Post-transcriptional ribosomal RNA (rRNA) modifications are present in all organisms, but their exact functional roles and positions are yet to be fully characterized. Modified nucleotides have been implicated in the stabilization of RNA structure and regulation of ribosome biogenesis and protein synthesis. In some instances, rRNA modifications can confer antibiotic resistance. High-resolution ribosome structures are thus necessary for precise determination of modified nucleotides' positions, a task that has previously been accomplished by X-ray crystallography. Here, we present a cryo-electron microscopy (cryo-EM) structure of the Escherichia coli 50S subunit at an average resolution of 2.2 Å as an additional approach for mapping modification sites. Our structure confirms known modifications present in 23S rRNA and additionally allows for localization of Mg2+ ions and their coordinated water molecules. Using our cryo-EM structure as a testbed, we developed a program for assessment of cryo-EM map quality. This program can be easily used on any RNA-containing cryo-EM structure, and an associated Coot plugin allows for visualization of validated modifications, making it highly accessible. PubMed: 31989172DOI: 10.1093/nar/gkaa037 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.2 Å) |
Structure validation
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