6TLX

Crystal structure of the unconventional kinetochore protein Perkinsela sp. KKT2a central domain

6TLX の概要

• エントリーDOI: 10.2210/pdb6tlx/pdb
• 関連するPDBエントリー: 6TLY
• 分子名称: Protein kinase, ZINC ION (2 entities in total)
• 機能のキーワード: kinetochore, zinc finger, kinetoplastid, kkt2, cell cycle
• 由来する生物種: Perkinsela sp. CCAP 1560/4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14701.35

構造登録者

Marciano, G.,Nerusheva, O.,Ishii, M.,Akiyoshi, B. (登録日: 2019-12-03, 公開日: 2019-12-25, 最終更新日: 2024-05-15)

主引用文献

Marciano, G.,Ishii, M.,Nerusheva, O.O.,Akiyoshi, B.
Kinetoplastid kinetochore proteins KKT2 and KKT3 have unique centromere localization domains.
J.Cell Biol., 220:-, 2021

PubMed Abstract: The kinetochore is the macromolecular protein complex that assembles onto centromeric DNA and binds spindle microtubules. Evolutionarily divergent kinetoplastids have an unconventional set of kinetochore proteins. It remains unknown how kinetochores assemble at centromeres in these organisms. Here, we characterize KKT2 and KKT3 in the kinetoplastid parasite Trypanosoma brucei. In addition to the N-terminal kinase domain and C-terminal divergent polo boxes, these proteins have a central domain of unknown function. We show that KKT2 and KKT3 are important for the localization of several kinetochore proteins and that their central domains are sufficient for centromere localization. Crystal structures of the KKT2 central domain from two divergent kinetoplastids reveal a unique zinc-binding domain (termed the CL domain for centromere localization), which promotes its kinetochore localization in T. brucei. Mutations in the equivalent domain in KKT3 abolish its kinetochore localization and function. Our work shows that the unique central domains play a critical role in mediating the centromere localization of KKT2 and KKT3.

PubMed: 34081090
DOI: 10.1083/jcb.202101022

実験手法

X-RAY DIFFRACTION (2.87 Å)