3MVD

Crystal structure of the chromatin factor RCC1 in complex with the nucleosome core particle

3MVD の概要

• エントリーDOI: 10.2210/pdb3mvd/pdb
• 関連するPDBエントリー: 1KX5 1ZLA
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total)
• 機能のキーワード: protein-dna complex, nucleosome core particle (ncp), ncp-chromatin factor complex, 7-bladed beta-propeller, signaling protein-structural protein-dna complex, signaling protein/structural protein/dna
• 由来する生物種: Xenopus laevis (clawed frog,common platanna,platanna); 詳細
• 細胞内の位置: Nucleus: P84233 P62799 P02281 P25171; Nucleus (By similarity): Q6AZJ8
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 289622.04

構造登録者

Makde, R.D.,England, J.R.,Yennawar, H.P.,Tan, S. (登録日: 2010-05-04, 公開日: 2010-08-25, 最終更新日: 2023-09-06)

主引用文献

Makde, R.D.,England, J.R.,Yennawar, H.P.,Tan, S.
Structure of RCC1 chromatin factor bound to the nucleosome core particle.
Nature, 467:562-566, 2010

PubMed Abstract: The small GTPase Ran enzyme regulates critical eukaryotic cellular functions including nuclear transport and mitosis through the creation of a RanGTP gradient around the chromosomes. This concentration gradient is created by the chromatin-bound RCC1 (regulator of chromosome condensation) protein, which recruits Ran to nucleosomes and activates Ran's nucleotide exchange activity. Although RCC1 has been shown to bind directly with the nucleosome, the molecular details of this interaction were not known. Here we determine the crystal structure of a complex of Drosophila RCC1 and the nucleosome core particle at 2.9 Å resolution, providing an atomic view of how a chromatin protein interacts with the histone and DNA components of the nucleosome. Our structure also suggests that the Widom 601 DNA positioning sequence present in the nucleosomes forms a 145-base-pair nucleosome core particle, not the expected canonical 147-base-pair particle.

PubMed: 20739938
DOI: 10.1038/nature09321

実験手法

X-RAY DIFFRACTION (2.9 Å)