1Q7F

Brain Tumor NHL domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.200 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Model of the Brain Tumor-Pumilio translation repressor complex

Edwards, T.A.Wilkinson, B.D.Wharton, R.P.Aggarwal, A.K.

(2003) Genes Dev 17: 2508-2513

  • DOI: https://doi.org/10.1101/gad.1119403
  • Primary Citation of Related Structures:  
    1Q7F

  • PubMed Abstract: 

    The Brain Tumor (Brat) protein is recruited to the 3' untranslated region (UTR) of hunchback mRNA to regulate its translation. Recruitment is mediated by interactions between the Pumilio RNA-binding Puf repeats and the NHL domain of Brat, a conserved structural motif present in a large family of growth regulators. In this report, we describe the crystal structure of the Brat NHL domain and present a model of the Pumilio-Brat complex derived from in silico docking experiments and supported by mutational analysis of the protein-protein interface. A key feature of the model is recognition of the outer, convex surface of the Pumilio Puf domain by the top, electropositive face of the six-bladed Brat beta-propeller. In particular, an extended loop in Puf repeat 8 fits in the entrance to the central channel of the Brat beta-propeller. Together, these interactions are likely to be prototypic of the recruitment strategies of other NHL-containing proteins in development.


  • Organizational Affiliation

    Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, New York 10029, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
brain tumor CG10719-PA
A, B
286Drosophila melanogasterMutation(s): 0 
Gene Names: brain tumor
UniProt
Find proteins for Q8MQJ9 (Drosophila melanogaster)
Explore Q8MQJ9 
Go to UniProtKB:  Q8MQJ9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8MQJ9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.200 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.77α = 90
b = 94.58β = 90
c = 130.5γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
SCALEPACKdata scaling
CNSrefinement
HKL-2000data reduction
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-10-21
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-31
    Changes: Experimental preparation
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references