8SWI

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

Summary for 8SWI

• Entry DOI: 10.2210/pdb8swi/pdb
• Descriptor: Eukaryotic huntingtin interacting protein B, Histone H3 peptided, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• Functional Keywords: ankyrin repeats, histone methyltransferase activity, cell invasion
• Biological source: Legionella pneumophila subsp. pneumophila; More
• Total number of polymer chains: 2
• Total formula weight: 53610.17

Authors

Xu, C.,Chung, I.Y.W.,Cygler, M. (deposition date: 2023-05-18, release date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3 Å)