9EVQ

Crystal structure of the kinetoplastid kinetochore protein KKT23 acetyltransferase domain from Trypanosoma brucei

9EVQ の概要

• エントリーDOI: 10.2210/pdb9evq/pdb
• 分子名称: N-acetyltransferase domain-containing protein, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: kinetochore, kinetoplastid, histone, acetyltransferase, mitosis, cell cycle
• 由来する生物種: Trypanosoma brucei brucei TREU927
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53861.26

構造登録者

Ludzia, P.,Ishii, M.,Akiyoshi, B. (登録日: 2024-04-01, 公開日: 2024-08-28, 最終更新日: 2025-01-15)

主引用文献

Ludzia, P.,Ishii, M.,Deak, G.,Spanos, C.,Wilson, M.D.,Redfield, C.,Akiyoshi, B.
The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail.
Structure, 33:123-, 2025

PubMed Abstract: The kinetochore is the macromolecular protein machine that drives chromosome segregation in eukaryotes. In an evolutionarily divergent group of organisms called kinetoplastids, kinetochores are built using a unique set of proteins (KKT1-25 and KKIP1-12). KKT23 is a constitutively localized kinetochore protein containing a C-terminal acetyltransferase domain of unknown function. Here, using X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, we have determined the structure and dynamics of the KKT23 acetyltransferase domain from Trypanosoma brucei and found that it is structurally similar to the GCN5 histone acetyltransferase domain. We find that KKT23 can acetylate the C-terminal tail of histone H2A and that knockdown of KKT23 results in decreased H2A acetylation levels in T. brucei. Finally, we have determined the crystal structure of the N-terminal region of KKT23 and shown that it interacts with KKT22. Our study provides important insights into the structure and function of the unique kinetochore acetyltransferase in trypanosomes.

PubMed: 39579771
DOI: 10.1016/j.str.2024.10.031

実験手法

X-RAY DIFFRACTION (1.75 Å)