4Z2M

Crystal structure of human SPT16 Mid-AID/H3-H4 tetramer FACT Histone complex

4Z2M の概要

• エントリーDOI: 10.2210/pdb4z2m/pdb
• 関連するPDBエントリー: 4Z2N
• 分子名称: FACT complex subunit SPT16, Histone H3.1, Histone H4 (3 entities in total)
• 機能のキーワード: transcription, transcription-dna binding protein complex, transcription/dna binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 79999.08

構造登録者

Tsunaka, Y.,Fujiwara, Y.,Oyama, T.,Hirose, S.,Morikawa, K. (登録日: 2015-03-30, 公開日: 2016-03-09, 最終更新日: 2023-11-08)

主引用文献

Tsunaka, Y.,Fujiwara, Y.,Oyama, T.,Hirose, S.,Morikawa, K.
Integrated molecular mechanism directing nucleosome reorganization by human FACT.
Genes Dev., 30:673-686, 2016

PubMed Abstract: Facilitates chromatin transcription (FACT) plays essential roles in chromatin remodeling during DNA transcription, replication, and repair. Our structural and biochemical studies of human FACT-histone interactions present precise views of nucleosome reorganization, conducted by the FACT-SPT16 (suppressor of Ty 16) Mid domain and its adjacent acidic AID segment. AID accesses the H2B N-terminal basic region exposed by partial unwrapping of the nucleosomal DNA, thereby triggering the invasion of FACT into the nucleosome. The crystal structure of the Mid domain complexed with an H3-H4 tetramer exhibits two separate contact sites; the Mid domain forms a novel intermolecular β structure with H4. At the other site, the Mid-H2A steric collision on the H2A-docking surface of the H3-H4 tetramer within the nucleosome induces H2A-H2B displacement. This integrated mechanism results in disrupting the H3 αN helix, which is essential for retaining the nucleosomal DNA ends, and hence facilitates DNA stripping from histone.

PubMed: 26966247
DOI: 10.1101/gad.274183.115

実験手法

X-RAY DIFFRACTION (2.981 Å)