5Y5A

Crystal structure of Est1 and Cdc13

Summary for 5Y5A

• Entry DOI: 10.2210/pdb5y5a/pdb
• Related: 5Y58 5Y59
• Descriptor: KLLA0F20702p, KLLA0F20922p (3 entities in total)
• Functional Keywords: telomerase, telomere, protein-protein complex, protein binding
• Biological source: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast); More
• Total number of polymer chains: 2
• Total formula weight: 69399.74

Authors

Chen, H.,Xue, J.,Wu, J.,Lei, M. (deposition date: 2017-08-08, release date: 2017-12-20, Last modification date: 2024-03-27)

Primary citation

Chen, H.,Xue, J.,Churikov, D.,Hass, E.P.,Shi, S.,Lemon, L.D.,Luciano, P.,Bertuch, A.A.,Zappulla, D.C.,Geli, V.,Wu, J.,Lei, M.
Structural Insights into Yeast Telomerase Recruitment to Telomeres
Cell, 172:331-343.e13, 2018

PubMed Abstract: Telomerase maintains chromosome ends from humans to yeasts. Recruitment of yeast telomerase to telomeres occurs through its Ku and Est1 subunits via independent interactions with telomerase RNA (TLC1) and telomeric proteins Sir4 and Cdc13, respectively. However, the structures of the molecules comprising these telomerase-recruiting pathways remain unknown. Here, we report crystal structures of the Ku heterodimer and Est1 complexed with their key binding partners. Two major findings are as follows: (1) Ku specifically binds to telomerase RNA in a distinct, yet related, manner to how it binds DNA; and (2) Est1 employs two separate pockets to bind distinct motifs of Cdc13. The N-terminal Cdc13-binding site of Est1 cooperates with the TLC1-Ku-Sir4 pathway for telomerase recruitment, whereas the C-terminal interface is dispensable for binding Est1 in vitro yet is nevertheless essential for telomere maintenance in vivo. Overall, our results integrate previous models and provide fundamentally valuable structural information regarding telomere biology.

PubMed: 29290466
DOI: 10.1016/j.cell.2017.12.008

Experimental method

X-RAY DIFFRACTION (2.206 Å)