5OSG

Structure of KSRP in context of Leishmania donovani 80S


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The cryo-EM Structure of a Novel 40S Kinetoplastid-Specific Ribosomal Protein.

Brito Querido, J.Mancera-Martinez, E.Vicens, Q.Bochler, A.Chicher, J.Simonetti, A.Hashem, Y.

(2017) Structure 25: 1785-1794.e3

  • DOI: 10.1016/j.str.2017.09.014
  • Primary Citation of Related Structures:  
    5OSG, 5OPT

  • 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 ...

    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.


    Related Citations: 
    • Structures and stabilization of kinetoplastid-specific split rRNAs revealed by comparing leishmanial and human ribosomes.
      Zhang, X., Lai, M., Chang, W., Yu, I., Ding, K., Mrazek, J., Ng, H.L., Yang, O.O., Maslov, D.A., Zhou, Z.H.
      (2016) Nat Commun 7: 13223

    Organizational Affiliation

    Université de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, UPR 9002, 67000 Strasbourg, France. Electronic address: y.hashem@ibmc-cnrs.unistra.fr.



Macromolecules

Find similar proteins by:  (by identity cutoff)  |  Structure
Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
RNA binding protein, putativeA [auth h]235Leishmania donovaniMutation(s): 0 
Gene Names: LDBPK_320790
Find proteins for E9BNI3 (Leishmania donovani (strain BPK282A1))
Explore E9BNI3 
Go to UniProtKB:  E9BNI3
Protein Feature View
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  Structure
Entity ID: 3
MoleculeChainsSequence LengthOrganismDetailsImage
40S ribosomal protein S6C [auth P]249Leishmania donovaniMutation(s): 0 
Gene Names: RPS6L3640.11Lmj_1130LmjF21.1780LmjF_21_1780
Find proteins for Q9NE83 (Leishmania major)
Explore Q9NE83 
Go to UniProtKB:  Q9NE83
Protein Feature View
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  • Reference Sequence
Find similar nucleic acids by:  (by identity cutoff)  |  Structure
Entity ID: 2
MoleculeChainsLengthOrganismImage
18S rRNAB [auth 2]2205Leishmania donovani
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
French National Research AgencyFranceANR-14-ACHN-0024
LABEXFranceANR-10-LABX-0036_NETRNA

Revision History  (Full details and data files)

  • Version 1.0: 2017-11-15
    Type: Initial release
  • Version 1.1: 2017-12-13
    Changes: Database references