8SWI

Crystal structure of legAS4 from Legionella pneumophila subsp. pneumophila with histone H3 (1-12)peptide

8SWI の概要

• エントリーDOI: 10.2210/pdb8swi/pdb
• 分子名称: Eukaryotic huntingtin interacting protein B, Histone H3 peptided, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: ankyrin repeats, histone methyltransferase activity, cell invasion
• 由来する生物種: Legionella pneumophila subsp. pneumophila; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53610.17

構造登録者

Xu, C.,Chung, I.Y.W.,Cygler, M. (登録日: 2023-05-18, 公開日: 2023-12-27)

主引用文献

Rolando, M.,Wah Chung, I.Y.,Xu, C.,Gomez-Valero, L.,England, P.,Cygler, M.,Buchrieser, C.
The SET and ankyrin domains of the secreted Legionella pneumophila histone methyltransferase work together to modify host chromatin.
Mbio, 14:e0165523-e0165523, 2023

PubMed Abstract: is an intracellular bacterium responsible of Legionnaires' disease, a severe pneumonia that is often fatal when not treated promptly. The pathogen's ability to efficiently colonize the host resides in its ability to replicate intracellularly. Essential for intracellular replication is translocation of many different protein effectors a specialized secretion system. One of them, called RomA, binds and directly modifies the host chromatin at a unique site (tri-methylation of lysine 14 of histone H3 [H3K14me]). However, the molecular mechanisms of binding are not known. Here, we resolve this question through structural characterization of RomA together with the H3 peptide. We specifically reveal an active role of the ankyrin repeats located in its C-terminal in the interaction with the histone H3 tail. Indeed, without the ankyrin domains, RomA loses its ability to act as histone methyltransferase. These results discover the molecular mechanisms by which a bacterial histone methyltransferase that is conserved in strains acts to modify chromatin.

PubMed: 37795993
DOI: 10.1128/mbio.01655-23

実験手法

X-RAY DIFFRACTION (3 Å)