5WAK

Crystal Structure of a Suz12-Rbbp4 Binary Complex

5WAK の概要

• エントリーDOI: 10.2210/pdb5wak/pdb
• 分子名称: Histone-binding protein RBBP4, Polycomb protein SUZ12, ZINC ION (3 entities in total)
• 機能のキーワード: methyltransferase, transcription
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus: Q09028 Q15022
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 105119.03

構造登録者

Chen, S.,Jiao, L.,Liu, X. (登録日: 2017-06-26, 公開日: 2018-03-14, 最終更新日: 2023-10-04)

主引用文献

Chen, S.,Jiao, L.,Shubbar, M.,Yang, X.,Liu, X.
Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding.
Mol. Cell, 69:840-852.e5, 2018

PubMed Abstract: Developmentally regulated accessory subunits dictate PRC2 function. Here, we report the crystal structures of a 120 kDa heterotetrameric complex consisting of Suz12, Rbbp4, Jarid2, and Aebp2 fragments that is minimally active in nucleosome binding and of an inactive binary complex of Suz12 and Rbbp4. Suz12 contains two unique structural platforms that define distinct classes of PRC2 holo complexes for chromatin binding. Aebp2 and Phf19 compete for binding of a non-canonical C2 domain of Suz12; Jarid2 and EPOP occupy an overlapped Suz12 surface required for chromatin association of PRC2. Suz12 and Aebp2 progressively block histone H3K4 binding to Rbbp4, suggesting that Rbbp4 may not be directly involved in PRC2 inhibition by the active H3K4me3 histone mark. Nucleosome binding enabled by Jarid2 and Aebp2 is in part accounted for by the structures, which also reveal that disruption of the Jarid2-Suz12 interaction may underlie the disease mechanism of an oncogenic chromosomal translocation of Suz12.

PubMed: 29499137
DOI: 10.1016/j.molcel.2018.01.039

実験手法

X-RAY DIFFRACTION (3.2 Å)