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5XXU

Small subunit of Toxoplasma gondii ribosome

Summary for 5XXU
Entry DOI10.2210/pdb5xxu/pdb
EMDB information6778 6780
Descriptor18S RNA, Ribosomal protein eS8, Ribosomal protein uS4, ... (34 entities in total)
Functional Keywordstoxoplasma gondii ribosome, rrna, rprotein, ribosome
Biological sourceToxoplasma gondii
More
Total number of polymer chains34
Total formula weight1177113.34
Authors
LI, Z.,Guo, Q.,Zheng, L.,Ji, Y.,Xie, Y.,Lai, D.,Lun, Z.,Suo, X.,Gao, N. (deposition date: 2017-07-05, release date: 2017-08-30, Last modification date: 2024-10-09)
Primary citationLi, 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: 28809395
DOI: 10.1038/cr.2017.104
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.35 Å)
Structure validation

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