2GHJ

Crystal structure of folded and partially unfolded forms of Aquifex aeolicus ribosomal protein L20


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.292 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.220 

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This is version 1.3 of the entry. See complete history


Literature

Coexistence of two protein folding states in the crystal structure of ribosomal protein L20

Timsit, Y.Allemand, F.Chiaruttini, C.Springer, M.

(2006) EMBO Rep 7: 1013-1018

  • DOI: https://doi.org/10.1038/sj.embor.7400803
  • Primary Citation of Related Structures:  
    2GHJ

  • PubMed Abstract: 

    The recent finding of intrinsically unstructured proteins defies the classical structure-function paradigm. However, owing to their flexibility, intrinsically unstructured proteins generally escape detailed structural investigations. Consequently little is known about the extent of conformational disorder and its role in biological functions. Here, we present the X-ray structure of the unbound ribosomal protein L20, the long basic amino-terminal extension of which has been previously interpreted as fully disordered in the absence of RNA. This study provides the first detailed picture of two protein folding states trapped together in a crystal and indicates that unfolding occurs in discrete regions of the whole protein, corresponding mainly to RNA-binding residues. The electrostatic destabilization of the long alpha-helix and a structural communication between the two L20 domains are reminiscent of those observed in calmodulin. The detailed comparison of the two conformations observed in the crystal provides new insights into the role of unfolded extensions in ribosomal assembly.


  • Organizational Affiliation

    Laboratoire de Cristallographie UPR9080, Institut de Biologie Physico-Chimique CNRS, 13, rue Pierre et Marie Curie, Paris 75005, France. timsit@ibpc.fr


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L20A,
B,
C [auth D],
D [auth E]
118Aquifex aeolicusMutation(s): 3 
Gene Names: rplT
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: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.292 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.220 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.914α = 104.06
b = 45.217β = 106.2
c = 67.06γ = 97.76
Software Package:
Software NamePurpose
MOSFLMdata reduction
CNSrefinement
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-04-18
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-02-07
    Changes: Experimental preparation