2BZF

Structural basis for DNA bridging by barrier-to-autointegration factor (BAF)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.87 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.244 
  • R-Value Observed: 0.244 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Structural Basis for DNA Bridging by Barrier-to-Autointegration Factor.

Bradley, C.M., Ronning, D.R., Ghirlando, R., Craigie, R., Dyda, F.

(2005) Nat Struct Mol Biol 12: 935

  • DOI: https://doi.org/10.1038/nsmb989
  • Primary Citation of Related Structures:  
    2BZF

  • PubMed Abstract: 

    The ability of barrier-to-autointegration factor (BAF) to bind and bridge DNA in a sequence-independent manner is crucial for its role in retroviral integration and a variety of cellular processes. To better understand this behavior, we solved the crystal structure of BAF bound to DNA. The structure reveals that BAF bridges DNA using two pairs of helix-hairpin-helix motifs located on opposite surfaces of the BAF dimer without changing its conformation.

    • Organizational Affiliation: 

    Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, US National Institutes of Health (NIH), 5 Center Drive, Bethesda, Maryland 20892, USA.


Macromolecules

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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BARRIER-TO-AUTOINTEGRATION FACTOR89Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for O75531 (Homo sapiens)
Explore O75531 
Go to UniProtKB:  O75531
PHAROS:  O75531
GTEx:  ENSG00000175334 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO75531
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
5'-D(*GP*TP*GP*GP*AP*GP*GP)-3'7N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 3
MoleculeChains LengthOrganismImage
5'-D(*CP*CP*TP*CP*CP*AP*CP)-3'7N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.87 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.244 
  • R-Value Observed: 0.244 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.83α = 90
b = 45.83β = 90
c = 241.92γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-09-15
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-13
    Changes: Data collection, Database references, Refinement description