5M0J

Crystal structure of the cytoplasmic complex with She2p, She3p, and the ASH1 mRNA E3-localization element


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.246 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.197 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex.

Edelmann, F.T.Schlundt, A.Heym, R.G.Jenner, A.Niedner-Boblenz, A.Syed, M.I.Paillart, J.C.Stehle, R.Janowski, R.Sattler, M.Jansen, R.P.Niessing, D.

(2017) Nat Struct Mol Biol 24: 152-161

  • DOI: https://doi.org/10.1038/nsmb.3351
  • Primary Citation of Related Structures:  
    5M0H, 5M0I, 5M0J

  • PubMed Abstract: 

    mRNA localization is an essential mechanism of gene regulation and is required for processes such as stem-cell division, embryogenesis and neuronal plasticity. It is not known which features in the cis-acting mRNA localization elements (LEs) are specifically recognized by motor-containing transport complexes. To the best of our knowledge, no high-resolution structure is available for any LE in complex with its cognate protein complex. Using X-ray crystallography and complementary techniques, we carried out a detailed assessment of an LE of the ASH1 mRNA from yeast, its complex with its shuttling RNA-binding protein She2p, and its highly specific, cytoplasmic complex with She3p. Although the RNA alone formed a flexible stem loop, She2p binding induced marked conformational changes. However, only joining by the unstructured She3p resulted in specific RNA recognition. The notable RNA rearrangements and joint action of a globular and an unfolded RNA-binding protein offer unprecedented insights into the step-wise maturation of an mRNA-transport complex.


  • Organizational Affiliation

    Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SWI5-dependent HO expression protein 2,SWI5-dependent HO expression protein 3328Saccharomyces cerevisiae RM11-1aMutation(s): 4 
Gene Names: SHE2SCRG_03894SHE3SCRG_02838
UniProt
Find proteins for P36068 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P36068 
Go to UniProtKB:  P36068
Find proteins for P38272 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P38272 
Go to UniProtKB:  P38272
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsP38272P36068
Sequence Annotations
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  • Reference Sequence
Find similar nucleic acids by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains LengthOrganismImage
ASH1 E3 (28 nt-loop)I [auth E],
J [auth F]
28Saccharomyces cerevisiae
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.246 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.197 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 219.03α = 90
b = 58.98β = 126.91
c = 144.68γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-01-18
    Type: Initial release
  • Version 1.1: 2017-01-25
    Changes: Database references
  • Version 1.2: 2017-02-15
    Changes: Database references
  • Version 1.3: 2024-01-17
    Changes: Data collection, Database references, Refinement description