1YFQ

High resolution S. cerevisiae Bub3 mitotic checkpoint protein

1YFQ の概要

• エントリーDOI: 10.2210/pdb1yfq/pdb
• 分子名称: Cell cycle arrest protein BUB3, CALCIUM ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: wd repeat wd40 repeat beta transducin repeat all beta, signaling protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus : P26449
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38799.96

構造登録者

Wilson, D.K.,Cerna, D.,Chew, E. (登録日: 2005-01-03, 公開日: 2005-01-11, 最終更新日: 2024-02-14)

主引用文献

Wilson, D.K.,Cerna, D.,Chew, E.
The 1.1-a structure of the spindle checkpoint protein bub3p reveals functional regions.
J.Biol.Chem., 280:13944-13951, 2005

PubMed Abstract: Bub3p is a protein that mediates the spindle checkpoint, a signaling pathway that ensures correct chromosome segregation in organisms ranging from yeast to mammals. It is known to function by co-localizing at least two other proteins, Mad3p and the protein kinase Bub1p, to the kinetochore of chromosomes that are not properly attached to mitotic spindles, ultimately resulting in cell cycle arrest. Prior sequence analysis suggested that Bub3p was composed of three or four WD repeats (also known as WD40 and beta-transducin repeats), short sequence motifs appearing in clusters of 4-16 found in many hundreds of eukaryotic proteins that fold into four-stranded blade-like sheets. We have determined the crystal structure of Bub3p from Saccharomyces cerevisiae at 1.1 angstrom and a crystallographic R-factor of 15.3%, revealing seven authentic repeats. In light of this, it appears that many of these repeats therefore remain hidden in sequences of other proteins. Analysis of random and site-directed mutants identifies the surface of Bub3p involved in checkpoint function through binding of Bub1p and Mad3p. Sequence alignments indicate that these surfaces are mostly conserved across Bub3 proteins from diverse species. A structural comparison with other proteins containing WD repeats suggests that these folds may bind partner proteins using similar surface areas on the top and sides of the propeller. The sequences composing these regions are the most divergent within the repeat across all WD repeat proteins and could potentially be modulated to provide specificity in partner protein binding without perturbation of the core structure.

PubMed: 15644329
DOI: 10.1074/jbc.M412919200

実験手法

X-RAY DIFFRACTION (1.1 Å)