5OSG

Structure of KSRP in context of Leishmania donovani 80S

Summary for 5OSG

• Entry DOI: 10.2210/pdb5osg/pdb
• Related: 5T2A
• EMDB information: 8343
• Descriptor: RNA binding protein, putative, 18S rRNA, 40S ribosomal protein S6 (3 entities in total)
• Functional Keywords: kinetoplastids, ribosome, cryo-em, ksrp
• Biological source: Leishmania donovani; More
• Total number of polymer chains: 3
• Total formula weight: 763896.57

Authors

Brito Querido, J.,Mancera-Martinez, E.,Vicens, Q.,Bochler, A.,Chicher, J.,Simonetti, A.,Hashem, Y. (deposition date: 2017-08-17, release date: 2017-11-15, Last modification date: 2024-05-08)

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

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: 29107485
DOI: 10.1016/j.str.2017.09.014

Experimental method

ELECTRON MICROSCOPY (2.9 Å)