2L9B

Heterodimer between Rna14p monkeytail domain and Rna15p hinge domain of the yeast CF IA complex


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Locked Tether Formation by Cooperative Folding of Rna14p Monkeytail and Rna15p Hinge Domains in the Yeast CF IA Complex.

Moreno-Morcillo, M.Minvielle-Sebastia, L.Fribourg, S.Mackereth, C.D.

(2011) Structure 19: 534-545

  • DOI: https://doi.org/10.1016/j.str.2011.02.003
  • Primary Citation of Related Structures:  
    2L9B

  • PubMed Abstract: 

    The removal of the 3' region of pre-mRNA followed by polyadenylation is a key step in mRNA maturation. In the yeast Saccharomyces cerevisiae, one component of the processing machinery is the cleavage/polyadenylation factor IA (CF IA) complex, composed of four proteins (Clp1p, Pcf11p, Rna14p, Rna15p) that recognize RNA sequences adjacent to the cleavage site and recruit additional processing factors. To gain insight into the molecular architecture of CF IA we solved the solution structure of the heterodimer composed of the interacting regions between Rna14p and Rna15p. The C-terminal monkeytail domain from Rna14p and the hinge region from Rna15p display a coupled binding and folding mechanism, where both peptides are initially disordered. Mutants with destabilized monkeytail-hinge interactions prevent association of Rna15p within CF IA. Conservation of interdomain residues reveals that the structural tethering is preserved in the homologous mammalian cleavage stimulation factor (CstF)-77 and CstF-64 proteins of the CstF complex.


  • Organizational Affiliation

    Institut Européen de Chimie et Biologie and INSERM U869, 33607 Pessac Cedex, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
mRNA 3'-end-processing protein RNA15109Saccharomyces cerevisiaeMutation(s): 1 
Gene Names: RNA15YGL044C
UniProt
Find proteins for P25299 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P25299 
Go to UniProtKB:  P25299
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP25299
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
mRNA 3'-end-processing protein RNA1453Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: RNA14YMR061WYM9796.14
UniProt
Find proteins for P25298 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P25298 
Go to UniProtKB:  P25298
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP25298
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-04-27
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-06-14
    Changes: Data collection, Database references, Other
  • Version 1.3: 2024-05-15
    Changes: Data collection, Database references