8sr6 | pdb_00008sr6

Crystal structure of legAS4 from Legionella pneumophila subsp. pneumophila with histone H3 (3-17)peptide

spinqualitylabelsall models 8sr6, resolution 2.22Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8sr6 is a 2 chain structure with sequence from Homo sapiens and Legionella pneumophila subsp. pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.22Å Ligands: EDO, GOL, K, PEG, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZUS4_LEGPH Publication Abstract from PubMed Legionella pneumophila 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 via 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 L. pneumophila strains acts to modify chromatin. The SET and ankyrin domains of the secreted Legionella pneumophila histone methyltransferase work together to modify host chromatin.,Rolando M, Wah Chung IY, Xu C, Gomez-Valero L, England P, Cygler M, Buchrieser C mBio. 2023 Oct 31;14(5):e0165523. doi: 10.1128/mbio.01655-23. Epub 2023 Oct 5. PMID:37795993 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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