6OM3

Crystal structure of the Orc1 BAH domain in complex with a nucleosome core particle

6OM3 の概要

• エントリーDOI: 10.2210/pdb6om3/pdb
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total)
• 機能のキーワード: chromatin modifier, structural protein, structural protein-dna complex, structural protein/dna
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 504285.53

構造登録者

De Ioannes, P.E.,Wang, M.,Armache, K.-J. (登録日: 2019-04-18, 公開日: 2019-07-10, 最終更新日: 2024-10-23)

主引用文献

De Ioannes, P.,Leon, V.A.,Kuang, Z.,Wang, M.,Boeke, J.D.,Hochwagen, A.,Armache, K.J.
Structure and function of the Orc1 BAH-nucleosome complex.
Nat Commun, 10:2894-2894, 2019

PubMed Abstract: The Origin Recognition Complex (ORC) is essential for replication, heterochromatin formation, telomere maintenance and genome stability in eukaryotes. Here we present the structure of the yeast Orc1 BAH domain bound to the nucleosome core particle. Our data reveal that Orc1, unlike its close homolog Sir3 involved in gene silencing, does not appear to discriminate between acetylated and non-acetylated lysine 16, modification states of the histone H4 tail that specify open and closed chromatin respectively. We elucidate the mechanism for this unique feature of Orc1 and hypothesize that its ability to interact with nucleosomes regardless of K16 modification state enables it to perform critical functions in both hetero- and euchromatin. We also show that direct interactions with nucleosomes are essential for Orc1 to maintain the integrity of rDNA borders during meiosis, a process distinct and independent from its known roles in silencing and replication.

PubMed: 31263106
DOI: 10.1038/s41467-019-10609-y

実験手法

X-RAY DIFFRACTION (3.3 Å)