2CJK

Structure of the RNA binding domain of Hrp1 in complex with RNA


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 25 
  • Selection Criteria: COMPARISON BETWEEN ENERGY- ORDERED RMSD PROFILES AND TOTAL ENERGY 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Grabbing the message: structural basis of mRNA 3'UTR recognition by Hrp1.

Perez-Canadillas, J.M.

(2006) EMBO J 25: 3167-3178

  • DOI: https://doi.org/10.1038/sj.emboj.7601190
  • Primary Citation of Related Structures:  
    2CJK

  • PubMed Abstract: 

    The recognition of specific signals encoded within the 3'-untranslated region of the newly transcribed mRNA triggers the assembly of a multiprotein machine that modifies its 3'-end. Hrp1 recognises one of such signals, the so-called polyadenylation enhancement element (PEE), promoting the recruitment of other polyadenylation factors in yeast. The molecular bases of this interaction are revealed here by the solution structure of a complex between Hrp1 and an oligonucleotide mimicking the PEE. Six consecutive bases (AUAUAU) are specifically recognised by two RNA-binding domains arranged in tandem. Both protein and RNA undergo significant conformational changes upon complex formation with a concomitant large surface burial of RNA bases. Key aspects of RNA specificity can be explained by the presence of intermolecular aromatic-aromatic contacts and hydrogen bonds. Altogether, the Hrp1-PEE structure represents one of the first steps towards understanding of the assembly of the cleavage and polyadenylation machinery at the atomic level.


  • Organizational Affiliation

    Laboratory of Molecular Biology, Medical Research Council, Cambridge, UK. jmperez@iqfr.csic.es


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEAR POLYADENYLATED RNA-BINDING PROTEIN 4167Saccharomyces cerevisiaeMutation(s): 0 
UniProt
Find proteins for Q99383 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q99383 
Go to UniProtKB:  Q99383
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ99383
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
5'-R(*UP*AP*UP*AP*UP*AP*UP*AP)-3'8Saccharomyces cerevisiae
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 25 
  • Selection Criteria: COMPARISON BETWEEN ENERGY- ORDERED RMSD PROFILES AND TOTAL ENERGY 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-06-28
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-05-02
    Changes: Data collection, Database references
  • Version 1.4: 2024-05-15
    Changes: Data collection, Database references