2RS6

Solution structure of the N-terminal dsRBD from RNA helicase A


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution structures of the double-stranded RNA-binding domains from RNA helicase A

Nagata, T.Tsuda, K.Kobayashi, N.Shirouzu, M.Kigawa, T.Guntert, P.Yokoyama, S.Muto, Y.

(2012) Proteins 80: 1699-1706

  • DOI: https://doi.org/10.1002/prot.24059
  • Primary Citation of Related Structures:  
    2RS6, 2RS7

  • PubMed Abstract: 

    RNA helicase A (RHA) is a highly conserved protein with multifaceted functions in the gene expression of cellular and viral mRNAs. RHA recognizes highly structured nucleotides and catalytically rearranges the various interactions between RNA, DNA, and protein molecules to provide a platform for the ribonucleoprotein complex. We present the first solution structures of the double-stranded RNA-binding domains (dsRBDs), dsRBD1 and dsRBD2, from mouse RHA. We discuss the binding mode of the dsRBDs of RHA, in comparison with the known dsRBD structures in their complexes. Our structural data provide important information for the elucidation of the molecular reassembly mediated by RHA.


  • Organizational Affiliation

    Institute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent RNA helicase A99Mus musculusMutation(s): 0 
Gene Names: Dhx9Ddx9
EC: 3.6.4.13
UniProt & NIH Common Fund Data Resources
Find proteins for O70133 (Mus musculus)
Explore O70133 
Go to UniProtKB:  O70133
IMPC:  MGI:108177
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO70133
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2012-03-14
    Type: Initial release
  • Version 1.1: 2013-10-16
    Changes: Database references
  • Version 1.2: 2023-06-14
    Changes: Data collection, Database references, Other
  • Version 1.3: 2024-05-15
    Changes: Data collection, Database references