7YDT

Crystal structure of mouse MPND

7YDT の概要

• エントリーDOI: 10.2210/pdb7ydt/pdb
• 分子名称: MPN domain containing protein (2 entities in total)
• 機能のキーワード: mpnd, dna binding protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34011.98

構造登録者

Yang, M.,Chen, Z. (登録日: 2022-07-04, 公開日: 2023-02-15, 最終更新日: 2024-05-29)

主引用文献

Yang, M.,Li, X.,Tian, Z.,Ma, L.,Ma, J.,Liu, Y.,Shang, G.,Liang, A.,Wu, W.,Chen, Z.
Structures of MPND Reveal the Molecular Recognition of Nucleosomes.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: Adenine N methylation in DNA (6mA) is a well-known epigenetic modification in bacteria, phages, and eukaryotes. Recent research has identified the Mpr1/Pad1 N-terminal (MPN) domain-containing protein (MPND) as a sensor protein that may recognize DNA 6mA modification in eukaryotes. However, the structural details of MPND and the molecular mechanism of their interaction remain unknown. Herein, we report the first crystal structures of the apo-MPND and MPND-DNA complex at resolutions of 2.06 Å and 2.47 Å, respectively. In solution, the assemblies of both apo-MPND and MPND-DNA are dynamic. In addition, MPND was found to possess the ability to bind directly to histones, no matter the N-terminal restriction enzyme-adenine methylase-associated domain or the C-terminal MPN domain. Moreover, the DNA and the two acidic regions of MPND synergistically enhance the interaction between MPND and histones. Therefore, our findings provide the first structural information regarding the MPND-DNA complex and also provide evidence of MPND-nucleosome interactions, thereby laying the foundation for further studies on gene control and transcriptional regulation.

PubMed: 36834777
DOI: 10.3390/ijms24043368

実験手法

X-RAY DIFFRACTION (2.055 Å)