1L1W

NMR structure of a SRP19 binding domain in human SRP RNA


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution structure of a SRP19 binding domain in human SRP RNA.

Sakamoto, T.Morita, S.Tabata, K.Nakamura, K.Kawai, G.

(2002) J Biochem 132: 177-182

  • DOI: https://doi.org/10.1093/oxfordjournals.jbchem.a003207
  • Primary Citation of Related Structures:  
    1L1W

  • PubMed Abstract: 

    Assembly of the human signal recognition particle (SRP) requires SRP19 protein to bind to helices 6 and 8 of SRP RNA. In the present study, structure of a 29-mer RNA composing the SRP19 binding site in helix 6 was determined by NMR spectroscopy. The two A:C mismatches were continuously stacked to each other and formed wobble type A:C base pairs. The GGAG tetraloop in helix 6 was found to adopt a similar conformation to that of GNRA tetraloop, suggesting that these tetraloops are included in an extensive new motif GNRR. Compared with the crystal structure of helix 6 in complex with SRP19 determined previously, the GGAG tetraloop in the complex was found to adopt a similar conformation to the free form, although the loop structure becomes more open upon SRP19 binding. Thus, SRP19 is thought to recognize the overall fold of the GGAG loop.


  • Organizational Affiliation

    Department of Industrial Chemistry, Faculty of Engineering, Chiba Institute of Technology, Narashino, Chiba 275-0016, Japan.


Macromolecules
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Entity ID: 1
MoleculeChains LengthOrganismImage
SRP19 binding domain of SRP RNA29N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-05-22
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Data collection, Database references, Derived calculations