2I91

60kDa Ro autoantigen in complex with a fragment of misfolded RNA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.65 Å
  • R-Value Free: 0.285 
  • R-Value Work: 0.241 
  • R-Value Observed: 0.245 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen.

Fuchs, G.Stein, A.J.Fu, C.Reinisch, K.M.Wolin, S.L.

(2006) Nat Struct Mol Biol 13: 1002-1009

  • DOI: https://doi.org/10.1038/nsmb1156
  • Primary Citation of Related Structures:  
    2I91

  • PubMed Abstract: 

    The Ro autoantigen is ring-shaped, binds misfolded noncoding RNAs and is proposed to function in quality control. Here we determine how Ro interacts with misfolded RNAs. Binding of Ro to misfolded precursor (pre)-5S ribosomal RNA requires a single-stranded 3' end and helical elements. As mutating most sequences of the helices and tail results in modest decreases in binding, Ro may be able to associate with a range of RNAs. Ro binds several other RNAs that contain single-stranded tails. A crystal structure of Ro bound to a misfolded pre-5S rRNA fragment reveals that the tail inserts into the cavity, while a helix binds on the surface. Most contacts of Ro with the helix are to the backbone. Mutagenesis reveals that Ro has an extensive RNA-binding surface. We propose that Ro uses this surface to scavenge RNAs that fail to bind their specific RNA-binding proteins.


  • Organizational Affiliation

    Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
60 kDa SS-A/Ro ribonucleoproteinE [auth A],
F [auth B]
538Xenopus laevisMutation(s): 0 
Gene Names: trove2
UniProt
Find proteins for P42700 (Xenopus laevis)
Explore P42700 
Go to UniProtKB:  P42700
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP42700
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
5'-R(*GP*CP*CP*UP*AP*CP*CP*C)-3'A [auth C],
C [auth E]
8N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
5'-R(*C*GP*GP*UP*AP*GP*GP*CP*UP*UP*UP*UP*CP*AP*A)-3'B [auth D],
D [auth F]
15N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.65 Å
  • R-Value Free: 0.285 
  • R-Value Work: 0.241 
  • R-Value Observed: 0.245 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.68α = 90
b = 119.98β = 98.91
c = 73.54γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-10-17
    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: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description