8CGL
Cryo-EM structure of RNase J from Helicobacter pylori
Summary for 8CGL
| Entry DOI | 10.2210/pdb8cgl/pdb |
| EMDB information | 16647 |
| Descriptor | Ribonuclease J (1 entity in total) |
| Functional Keywords | ribonuclease, rnase j, degradosome, helicobacter pylori, rna binding protein |
| Biological source | Helicobacter pylori B128 |
| Total number of polymer chains | 4 |
| Total formula weight | 316787.72 |
| Authors | |
| Primary citation | Tejada-Arranz, A.,Lulla, A.,Bouilloux-Lafont, M.,Turlin, E.,Pei, X.Y.,Douche, T.,Matondo, M.,Williams, A.H.,Raynal, B.,Luisi, B.F.,De Reuse, H. Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease. Nat Commun, 14:8072-8072, 2023 Cited by PubMed Abstract: In the gastric pathogen Helicobacter pylori, post-transcriptional regulation relies strongly on the activity of the essential ribonuclease RNase J. Here, we elucidated the crystal and cryo-EM structures of RNase J and determined that it assembles into dimers and tetramers in vitro. We found that RNase J extracted from H. pylori is acetylated on multiple lysine residues. Alanine substitution of several of these residues impacts on H. pylori morphology, and thus on RNase J function in vivo. Mutations of Lysine 649 modulates RNase J oligomerization in vitro, which in turn influences ribonuclease activity in vitro. Our structural analyses of RNase J reveal loops that gate access to the active site and rationalizes how acetylation state of K649 can influence activity. We propose acetylation as a regulatory level controlling the activity of RNase J and its potential cooperation with other enzymes of RNA metabolism in H. pylori. PubMed: 38057323DOI: 10.1038/s41467-023-43825-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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