Summary for 5XY3
| Entry DOI | 10.2210/pdb5xy3/pdb |
| EMDB information | 6784 |
| Descriptor | 25S ribosomal RNA, Ribosomal protein L7Ae, putative, Ribosomal protein L6, putative, ... (43 entities in total) |
| Functional Keywords | trichomonas vaginalis ribosome, rrna, rprotein, ribosome |
| Biological source | Trichomonas vaginalis More |
| Total number of polymer chains | 43 |
| Total formula weight | 1713540.10 |
| Authors | |
| Primary citation | Li, Z.,Guo, Q.,Zheng, L.,Ji, Y.,Xie, Y.T.,Lai, D.H.,Lun, Z.R.,Suo, X.,Gao, N. Cryo-EM structures of the 80S ribosomes from human parasites Trichomonas vaginalis and Toxoplasma gondii Cell Res., 27:1275-1288, 2017 Cited by PubMed Abstract: As an indispensable molecular machine universal in all living organisms, the ribosome has been selected by evolution to be the natural target of many antibiotics and small-molecule inhibitors. High-resolution structures of pathogen ribosomes are crucial for understanding the general and unique aspects of translation control in disease-causing microbes. With cryo-electron microscopy technique, we have determined structures of the cytosolic ribosomes from two human parasites, Trichomonas vaginalis and Toxoplasma gondii, at resolution of 3.2-3.4 Å. Although the ribosomal proteins from both pathogens are typical members of eukaryotic families, with a co-evolution pattern between certain species-specific insertions/extensions and neighboring ribosomal RNA (rRNA) expansion segments, the sizes of their rRNAs are sharply different. Very interestingly, rRNAs of T. vaginalis are in size comparable to prokaryotic counterparts, with nearly all the eukaryote-specific rRNA expansion segments missing. These structures facilitate the dissection of evolution path for ribosomal proteins and RNAs, and may aid in design of novel translation inhibitors. PubMed: 28809395DOI: 10.1038/cr.2017.104 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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