3K0X

Crystal structure of telomere capping protein Ten1 from Saccharomyces pombe


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.188 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain.

Gelinas, A.D.Paschini, M.Reyes, F.E.Heroux, A.Batey, R.T.Lundblad, V.Wuttke, D.S.

(2009) Proc Natl Acad Sci U S A 106: 19298-19303

  • DOI: https://doi.org/10.1073/pnas.0909203106
  • Primary Citation of Related Structures:  
    3K0X, 3K10

  • PubMed Abstract: 

    Telomeres must be capped to preserve chromosomal stability. The conserved Stn1 and Ten1 proteins are required for proper capping of the telomere, although the mechanistic details of how they contribute to telomere maintenance are unclear. Here, we report the crystal structures of the C-terminal domain of the Saccharomyces cerevisiae Stn1 and the Schizosaccharomyces pombe Ten1 proteins. These structures reveal striking similarities to corresponding subunits in the replication protein A complex, further supporting an evolutionary link between telomere maintenance proteins and DNA repair complexes. Our structural and in vivo data of Stn1 identify a new domain that has evolved to support a telomere-specific role in chromosome maintenance. These findings endorse a model of an evolutionarily conserved mechanism of DNA maintenance that has developed as a result of increased chromosomal structural complexity.


  • Organizational Affiliation

    Department of Chemistry and Biochemistry, University of Colorado, UCB 215, Boulder, CO 80309-0125, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein Ten1102Schizosaccharomyces pombeMutation(s): 0 
Gene Names: SPCC1393.14ten1
UniProt
Find proteins for P0C5Y7 (Schizosaccharomyces pombe (strain 972 / ATCC 24843))
Explore P0C5Y7 
Go to UniProtKB:  P0C5Y7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0C5Y7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.188 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.304α = 90
b = 64.304β = 90
c = 66.242γ = 120
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RESOLVEphasing
CNSrefinement
PDB_EXTRACTdata extraction
CrystalCleardata collection

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-10-27
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-02-21
    Changes: Data collection, Database references, Derived calculations