5OPT
Structure of KSRP in context of Trypanosoma cruzi 40S
Summary for 5OPT
| Entry DOI | 10.2210/pdb5opt/pdb |
| EMDB information | 3844 |
| Descriptor | Activated protein kinase C receptor, putative, 40S ribosomal protein S13, putative, 40S ribosomal protein S27, putative, ... (35 entities in total) |
| Functional Keywords | kinetoplastids, ribosome, cryo-em, ksrp |
| Biological source | Trypanosoma cruzi (strain CL Brener) More |
| Cellular location | Cytoplasm : Q4DZ41 Q4CQ63 |
| Total number of polymer chains | 35 |
| Total formula weight | 1416991.87 |
| Authors | Brito Querido, J.,Mancera-Martinez, E.,Vicens, Q.,Bochler, A.,Chicher, J.,Simonetti, A.,Hashem, Y. (deposition date: 2017-08-10, release date: 2017-11-15, Last modification date: 2024-11-20) |
| Primary citation | Brito Querido, J.,Mancera-Martinez, E.,Vicens, Q.,Bochler, A.,Chicher, J.,Simonetti, A.,Hashem, Y. The cryo-EM Structure of a Novel 40S Kinetoplastid-Specific Ribosomal Protein. Structure, 25:1785-1794.e3, 2017 Cited by PubMed Abstract: Kinetoplastids are potentially lethal protozoan pathogens affecting more than 20 million people worldwide. There is a critical need for more specific targets for the development of safer anti-kinetoplastid therapeutic molecules that can replace the scarce and highly cytotoxic current drugs. The kinetoplastid ribosome represents a potential therapeutic target due to its relative structural divergence when compared with its human counterpart. However, several kinetoplastid-specific ribosomal features remain uncharacterized. Here, we present the near-atomic cryoelectron microscopy structure of a novel bona fide kinetoplastid-specific ribosomal (r-) protein (KSRP) bound to the ribosome. KSRP is an essential protein located at the solvent face of the 40S subunit, where it binds and stabilizes kinetoplastid-specific domains of rRNA, suggesting its role in ribosome integrity. KSRP also interacts with the r-protein eS6 at a region that is only conserved in kinetoplastids. The kinetoplastid-specific ribosomal environment of KSRP provides a promising target for the design of safer anti-kinetoplastidian drugs. PubMed: 29107485DOI: 10.1016/j.str.2017.09.014 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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