1U63

THE STRUCTURE OF A RIBOSOMAL PROTEIN L1-mRNA COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.302 
  • R-Value Work: 0.276 
  • R-Value Observed: 0.276 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA.

Nevskaya, N.Tishchenko, S.Gabdoulkhakov, A.Nikonova, E.Nikonov, O.Nikulin, A.Platonova, O.Garber, M.Nikonov, S.Piendl, W.

(2005) Nucleic Acids Res 33: 478-485

  • DOI: https://doi.org/10.1093/nar/gki194
  • Primary Citation of Related Structures:  
    1U63

  • PubMed Abstract: 

    The RNA-binding ability of ribosomal protein L1 is of profound interest since the protein has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding its mRNA. Here, we report the crystal structure of ribosomal protein L1 in complex with a specific fragment of its mRNA and compare it with the structure of L1 in complex with a specific fragment of 23S rRNA determined earlier. In both complexes, a strongly conserved RNA structural motif is involved in L1 binding through a conserved network of RNA-protein H-bonds inaccessible to the solvent. These interactions should be responsible for specific recognition between the protein and RNA. A large number of additional non-conserved RNA-protein H-bonds stabilizes both complexes. The added contribution of these non-conserved H-bonds makes the ribosomal complex much more stable than the regulatory one.


  • Organizational Affiliation

    Institute of Protein Research, Russian Academy of Sciences 142290 Pushchino, Moscow region, Russia.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L1PC [auth A],
D [auth C]
219Methanocaldococcus jannaschiiMutation(s): 6 
Gene Names: rpl1p
UniProt
Find proteins for P54050 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440))
Explore P54050 
Go to UniProtKB:  P54050
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP54050
Sequence Annotations
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  • Reference Sequence
Find similar nucleic acids by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains LengthOrganismImage
49 NT FRAGMENT OF MRNA FOR L1A [auth B],
B [auth D]
49N/A
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
C [auth A],
D [auth C]
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.302 
  • R-Value Work: 0.276 
  • R-Value Observed: 0.276 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 212.29α = 90
b = 68.9β = 122.99
c = 115.87γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
XDSdata scaling
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-04-12
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2016-11-30
    Changes: Other