1GYZ

Bacterial ribosomal protein L20 from Aquifex aeolicus


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: LOWEST DIANA TARGET FUNCTION 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

NMR Structure of Bacterial Ribosomal Protein L20: Implications for Ribosome Assembly and Translational Control

Raibaud, S.Lebars, I.Guillier, M.Chiaruttini, C.Bontems, F.Rak, A.Garber, M.Allemand, F.Springer, M.Dardel, F.

(2002) J Mol Biol 323: 143

  • DOI: https://doi.org/10.1016/s0022-2836(02)00921-x
  • Primary Citation of Related Structures:  
    1GYZ

  • PubMed Abstract: 

    L20 is a specific protein of the bacterial ribosome, which is involved in the early assembly steps of the 50S subunit and in the feedback control of the expression of its own gene. This dual function involves specific interactions with either the 23S rRNA or its messenger RNA. The solution structure of the free Aquifex aeolicus L20 has been solved. It is composed of an unstructured N-terminal domain comprising residues 1-58 and a C-terminal alpha-helical domain. This is in contrast with what is observed in the bacterial 50S subunit, where the N-terminal region folds as an elongated alpha-helical region. The solution structure of the C-terminal domain shows that several solvent-accessible, conserved residues are clustered on the surface of the molecule and are probably involved in RNA recognition. In vivo studies show that this domain is sufficient to repress the expression of the cistrons encoding L35 and L20 in the IF3 operon. The ability of L20 C-terminal domain to specifically recognise RNA suggests an assembly mechanism for L20 into the ribosome. The pre-folded C-terminal domain would make a primary interaction with a specific site on the 23S rRNA. The N-terminal domain would then fold within the ribosome, participating in its correct 3D assembly.


  • Organizational Affiliation

    Cristallographie et RMN Biologiques, UMR 8015 CNRS, Faculté de Pharmacie, 4 avenue de l'Observatoire, 75006 Paris, France.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
50S RIBOSOMAL PROTEIN L2060Aquifex aeolicus VF5Mutation(s): 0 
UniProt
Find proteins for O67086 (Aquifex aeolicus (strain VF5))
Explore O67086 
Go to UniProtKB:  O67086
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO67086
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: LOWEST DIANA TARGET FUNCTION 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-05-10
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance