1A5J

CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 32 
  • Selection Criteria: NO DISTANCE CONSTRAINT ORVAN DER WAALS VIOLATIONS >0.5A,NO DIHEDRAL ANGLE CONSTRAINT VIOLATIONS >6 DEGREES 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression.

McIntosh, P.B.Frenkiel, T.A.Wollborn, U.McCormick, J.E.Klempnauer, K.H.Feeney, J.Carr, M.D.

(1998) Biochemistry 37: 9619-9629

  • DOI: https://doi.org/10.1021/bi972861z
  • Primary Citation of Related Structures:  
    1A5J

  • PubMed Abstract: 

    Double- and triple-resonance heteronuclear NMR spectroscopy have been used to determine the high-resolution solution structure of the minimal B-Myb DNA-binding domain (B-MybR2R3) and to characterize the specific complex formed with a synthetic DNA fragment corresponding to the Myb target site on the Myb-regulated gene tom-1. B-MybR2R3 is shown to consist of two independent protein domains (R2 and R3) joined by a short linker, which have strikingly different tertiary structures despite significant sequence similarities. In addition, the C-terminal region of B-Myb R2 is confirmed to have a poorly defined structure, reflecting the existence of multiple conformations in slow to intermediate exchange. This contrasts with the tertiary structure reported for c-MybR2R3, in which both R2 and R3 have the same fold and the C-terminal region of R2 forms a stable, well-defined helix [Ogata, K., et al. (1995) Nat. Struct. Biol. 2, 309-320]. The NMR data suggest there are extensive contacts between B-MybR2R3 and its DNA target site in the complex and are consistent with a significant conformational change in the protein on binding to DNA, with one possibility being the formation of a stable helix in the C-terminal region of R2. In addition, conformational heterogeneity identified in R2 of B-MybR2R3 bound to the tom-1-A target site may play an important role in the control of gene expression by Myb proteins.


  • Organizational Affiliation

    Laboratory of Molecular Structure, National Institute for Biological Standards and Control, Potters Bar, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
B-MYB110Gallus gallusMutation(s): 0 
UniProt
Find proteins for Q03237 (Gallus gallus)
Explore Q03237 
Go to UniProtKB:  Q03237
Entity Groups  
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UniProt GroupQ03237
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 32 
  • Selection Criteria: NO DISTANCE CONSTRAINT ORVAN DER WAALS VIOLATIONS >0.5A,NO DIHEDRAL ANGLE CONSTRAINT VIOLATIONS >6 DEGREES 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-07-01
    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: 2022-02-16
    Changes: Database references, Derived calculations, Other, Structure summary
  • Version 1.4: 2024-05-22
    Changes: Data collection