3VH5

Crystal structure of the chicken CENP-T histone fold/CENP-W/CENP-S/CENP-X heterotetrameric complex, crystal form I

3VH5 の概要

• エントリーDOI: 10.2210/pdb3vh5/pdb
• 関連するPDBエントリー: 3VH6
• 分子名称: CENP-S, CENP-X, CENP-T, ... (5 entities in total)
• 機能のキーワード: histone fold, chromosome segregation, dna binding, nucleus, dna binding protein
• 由来する生物種: Gallus gallus (chicken); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46461.55

構造登録者

Nishino, T.,Takeuchi, K.,Gascoigne, K.E.,Suzuki, A.,Hori, T.,Oyama, T.,Morikawa, K.,Cheeseman, I.M.,Fukagawa, T. (登録日: 2011-08-23, 公開日: 2012-03-07, 最終更新日: 2023-11-08)

主引用文献

Nishino, T.,Takeuchi, K.,Gascoigne, K.E.,Suzuki, A.,Hori, T.,Oyama, T.,Morikawa, K.,Cheeseman, I.M.,Fukagawa, T.
CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold
Cell(Cambridge,Mass.), 148:487-501, 2012

PubMed Abstract: The multiprotein kinetochore complex must assemble at a specific site on each chromosome to achieve accurate chromosome segregation. Defining the nature of the DNA-protein interactions that specify the position of the kinetochore and provide a scaffold for kinetochore formation remain key goals. Here, we demonstrate that the centromeric histone-fold-containing CENP-T-W and CENP-S-X complexes coassemble to form a stable CENP-T-W-S-X heterotetramer. High-resolution structural analysis of the individual complexes and the heterotetramer reveals similarity to other histone fold-containing complexes including canonical histones within a nucleosome. The CENP-T-W-S-X heterotetramer binds to and supercoils DNA. Mutants designed to compromise heterotetramerization or the DNA-protein contacts around the heterotetramer strongly reduce the DNA binding and supercoiling activities in vitro and compromise kinetochore assembly in vivo. These data suggest that the CENP-T-W-S-X complex forms a unique nucleosome-like structure to generate contacts with DNA, extending the "histone code" beyond canonical nucleosome proteins.

PubMed: 22304917
DOI: 10.1016/j.cell.2011.11.061

実験手法

X-RAY DIFFRACTION (2.402 Å)