2GCC

SOLUTION STRUCTURE OF THE GCC-BOX BINDING DOMAIN, NMR, MINIMIZED MEAN STRUCTURE


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 
  • Conformers Submitted: 
  • Selection Criteria: NO NOE VIOLATIONS 

wwPDB Validation   3D Report Full Report

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This is version 1.3 of the entry. See complete history


Literature

A novel mode of DNA recognition by a beta-sheet revealed by the solution structure of the GCC-box binding domain in complex with DNA.

Allen, M.D.Yamasaki, K.Ohme-Takagi, M.Tateno, M.Suzuki, M.

(1998) EMBO J 17: 5484-5496

  • DOI: https://doi.org/10.1093/emboj/17.18.5484
  • Primary Citation of Related Structures:  
    1GCC, 2GCC, 3GCC

  • PubMed Abstract: 

    The 3D solution structure of the GCC-box binding domain of a protein from Arabidopsis thaliana in complex with its target DNA fragment has been determined by heteronuclear multidimensional NMR in combination with simulated annealing and restrained molecular dynamic calculation. The domain consists of a three-stranded anti-parallel beta-sheet and an alpha-helix packed approximately parallel to the beta-sheet. Arginine and tryptophan residues in the beta-sheet are identified to contact eight of the nine consecutive base pairs in the major groove, and at the same time bind to the sugar phosphate backbones. The target DNA bends slightly at the central CG step, thereby allowing the DNA to follow the curvature of the beta-sheet.


  • Organizational Affiliation

    AIST-NIBHT Plant Molecular Biology Laboratory, Higashi 1-1, Tsukuba 305-0046, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATERF170Arabidopsis thalianaMutation(s): 0 
Gene Names: ATERF1
UniProt
Find proteins for O80337 (Arabidopsis thaliana)
Explore O80337 
Go to UniProtKB:  O80337
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO80337
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 
  • Conformers Submitted: 
  • Selection Criteria: NO NOE VIOLATIONS 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-03-23
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-09
    Changes: Database references, Derived calculations, Other