3K0X

Crystal structure of telomere capping protein Ten1 from Saccharomyces pombe

Summary for 3K0X

• Entry DOI: 10.2210/pdb3k0x/pdb
• Related: 3K10
• Descriptor: Protein Ten1, IODIDE ION (3 entities in total)
• Functional Keywords: beta barrel, ob fold, telomere capping, chromosomal protein, nucleus, telomere, protein binding
• Biological source: Schizosaccharomyces pombe (yeast)
• Cellular location: Nucleus: P0C5Y7
• Total number of polymer chains: 1
• Total formula weight: 12564.67

Authors

Gelinas, A.D.,Reyes, F.E.,Batey, R.T.,Wuttke, D.S. (deposition date: 2009-09-25, release date: 2009-10-27, Last modification date: 2024-02-21)

Primary citation

Gelinas, A.D.,Paschini, M.,Reyes, F.E.,Heroux, A.,Batey, R.T.,Lundblad, V.,Wuttke, D.S.
Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain.
Proc.Natl.Acad.Sci.USA, 106:19298-19303, 2009

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.

PubMed: 19884503
DOI: 10.1073/pnas.0909203106

Experimental method

X-RAY DIFFRACTION (1.7 Å)