1IYJ

STRUCTURE OF A BRCA2-DSS1 COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.295 
  • R-Value Work: 0.244 
  • R-Value Observed: 0.248 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure.

Yang, H.Jeffrey, P.D.Miller, J.Kinnucan, E.Sun, Y.Thoma, N.H.Zheng, N.Chen, P.L.Lee, W.H.Pavletich, N.P.

(2002) Science 297: 1837-1848

  • DOI: https://doi.org/10.1126/science.297.5588.1837
  • Primary Citation of Related Structures:  
    1IYJ, 1MIU, 1MJE

  • PubMed Abstract: 

    Mutations in the BRCA2 (breast cancer susceptibility gene 2) tumor suppressor lead to chromosomal instability due to defects in the repair of double-strand DNA breaks (DSBs) by homologous recombination, but BRCA2's role in this process has been unclear. Here, we present the 3.1 angstrom crystal structure of a approximately 90-kilodalton BRCA2 domain bound to DSS1, which reveals three oligonucleotide-binding (OB) folds and a helix-turn-helix (HTH) motif. We also (i) demonstrate that this BRCA2 domain binds single-stranded DNA, (ii) present its 3.5 angstrom structure bound to oligo(dT)9, (iii) provide data that implicate the HTH motif in dsDNA binding, and (iv) show that BRCA2 stimulates RAD51-mediated recombination in vitro. These findings establish that BRCA2 functions directly in homologous recombination and provide a structural and biochemical basis for understanding the loss of recombination-mediated DSB repair in BRCA2-associated cancers.


  • Organizational Affiliation

    Department of Pharmacology, Sloan-Kettering Division, Joan and Sanford I. Weill Graduate School of Medical Sciences, Cornell University, New York, NY 10021, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Deleted in split hand/split foot protein 1
A, C
70Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P60896 (Homo sapiens)
Explore P60896 
Go to UniProtKB:  P60896
PHAROS:  P60896
GTEx:  ENSG00000127922 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP60896
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
breast cancer susceptibility
B, D
817Rattus norvegicusMutation(s): 0 
UniProt
Find proteins for O35923 (Rattus norvegicus)
Explore O35923 
Go to UniProtKB:  O35923
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO35923
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.295 
  • R-Value Work: 0.244 
  • R-Value Observed: 0.248 
  • Space Group: P 43
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 130.314α = 90
b = 130.314β = 90
c = 192.615γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNSrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-10-02
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references