6NFX

MBTD1 MBT repeats

6NFX の概要

• エントリーDOI: 10.2210/pdb6nfx/pdb
• 分子名称: MBT domain-containing protein 1,Enhancer of polycomb homolog 1, UNKNOWN ATOM OR ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: mbt domain, protein binding, structural genomics, structural genomics consortium, sgc
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52378.54

構造登録者

Zhang, H.,Tempel, W.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2018-12-21, 公開日: 2019-01-30, 最終更新日: 2023-10-11)

主引用文献

Zhang, H.,Devoucoux, M.,Song, X.,Li, L.,Ayaz, G.,Cheng, H.,Tempel, W.,Dong, C.,Loppnau, P.,Cote, J.,Min, J.
Structural Basis for EPC1-Mediated Recruitment of MBTD1 into the NuA4/TIP60 Acetyltransferase Complex.
Cell Rep, 30:3996-4002.e4, 2020

PubMed Abstract: MBTD1, a H4K20me reader, has recently been identified as a component of the NuA4/TIP60 acetyltransferase complex, regulating gene expression and DNA repair. NuA4/TIP60 inhibits 53BP1 binding to chromatin through recognition of the H4K20me mark by MBTD1 and acetylation of H2AK15, blocking the ubiquitination mark required for 53BP1 localization at DNA breaks. The NuA4/TIP60 non-catalytic subunit EPC1 enlists MBTD1 into the complex, but the detailed molecular mechanism remains incompletely explored. Here, we present the crystal structure of the MBTD1-EPC1 complex, revealing a hydrophobic C-terminal fragment of EPC1 engaging the MBT repeats of MBTD1 in a site distinct from the H4K20me binding site. Different cellular assays validate the physiological significance of the key residues involved in the MBTD1-EPC1 interaction. Our study provides a structural framework for understanding the mechanism by which MBTD1 recruits the NuA4/TIP60 acetyltransferase complex to influence transcription and DNA repair pathway choice.

PubMed: 32209463
DOI: 10.1016/j.celrep.2020.03.003

実験手法

X-RAY DIFFRACTION (1.95 Å)