6ZPK

Crystal structure of the unconventional kinetochore protein Trypanosoma brucei KKT4 BRCT domain

6ZPK の概要

• エントリーDOI: 10.2210/pdb6zpk/pdb
• 分子名称: Trypanosoma brucei KKT4 463-645, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: kinetochore, kinetoplastid, kkt4, brct, cell cycle
• 由来する生物種: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20319.13

構造登録者

Ludzia, P.,Lowe, E.D.,Marciano, G.,Mohammed, S.,Redfield, C.,Akiyoshi, B. (登録日: 2020-07-08, 公開日: 2020-10-21, 最終更新日: 2024-06-19)

主引用文献

Ludzia, P.,Lowe, E.D.,Marciano, G.,Mohammed, S.,Redfield, C.,Akiyoshi, B.
Structural characterization of KKT4, an unconventional microtubule-binding kinetochore protein.
Structure, 29:1014-1028.e8, 2021

PubMed Abstract: The kinetochore is the macromolecular machinery that drives chromosome segregation by interacting with spindle microtubules. Kinetoplastids (such as Trypanosoma brucei), a group of evolutionarily divergent eukaryotes, have a unique set of kinetochore proteins that lack any significant homology to canonical kinetochore components. To date, KKT4 is the only kinetoplastid kinetochore protein that is known to bind microtubules. Here we use X-ray crystallography, NMR spectroscopy, and crosslinking mass spectrometry to characterize the structure and dynamics of KKT4. We show that its microtubule-binding domain consists of a coiled-coil structure followed by a positively charged disordered tail. The structure of the C-terminal BRCT domain of KKT4 reveals that it is likely a phosphorylation-dependent protein-protein interaction domain. The BRCT domain interacts with the N-terminal region of the KKT4 microtubule-binding domain and with a phosphopeptide derived from KKT8. Taken together, these results provide structural insights into the unconventional kinetoplastid kinetochore protein KKT4.

PubMed: 33915106
DOI: 10.1016/j.str.2021.04.004

実験手法

X-RAY DIFFRACTION (1.57 Å)