5XXF

Crystal structure of Poz1, Tpz1 and Rap1

Summary for 5XXF

• Entry DOI: 10.2210/pdb5xxf/pdb
• Related: 5XXE
• Descriptor: Protection of telomeres protein poz1, Protection of telomeres protein tpz1, Rap1, ... (5 entities in total)
• Functional Keywords: telomere, sheterin, hub, dna binding protein
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast); More
• Cellular location: Cytoplasm : O13852; Chromosome, telomere : O14246
• Total number of polymer chains: 6
• Total formula weight: 70587.73

Authors

Xue, J.,Chen, H.,Wu, J.,Lei, M. (deposition date: 2017-07-03, release date: 2017-12-20, Last modification date: 2023-11-22)

Primary citation

Xue, J.,Chen, H.,Wu, J.,Takeuchi, M.,Inoue, H.,Liu, Y.,Sun, H.,Chen, Y.,Kanoh, J.,Lei, M.
Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex.
Cell Res., 27:1503-1520, 2017

PubMed Abstract: Telomeric shelterin complex caps chromosome ends and plays a crucial role in telomere maintenance and protection. In the fission yeast Schizosaccharomyces pombe, shelterin is composed of telomeric single- and double-stranded DNA-binding protein subcomplexes Pot1-Tpz1 and Taz1-Rap1, which are bridged by their interacting protein Poz1. However, the structure of Poz1 and how Poz1 functions as an interaction hub in the shelterin complex remain unclear. Here we report the crystal structure of Poz1 in complex with Poz1-binding motifs of Tpz1 and Rap1. The crystal structure shows that Poz1 employs two different binding surfaces to interact with Tpz1 and Rap1. Unexpectedly, the structure also reveals that Poz1 adopts a dimeric conformation. Mutational analyses suggest that proper interactions between Tpz1, Poz1, and Rap1 in the shelterin core complex are required for telomere length homeostasis and heterochromatin structure maintenance at telomeres. Structural resemblance between Poz1 and the TRFH domains of other shelterin proteins in fission yeast and humans suggests a model for the evolution of shelterin proteins.

PubMed: 29160296
DOI: 10.1038/cr.2017.145

Experimental method

X-RAY DIFFRACTION (3.1 Å)