9bdp | pdb_00009bdp

80S ribosome bound with angiogenin and complex of eEF1A and Ala-tRNAAla

spinqualitylabelsall models 9bdp, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9bdp is a 10 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL8_RABIT Component of the large ribosomal subunit (PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). Publication Abstract from PubMed Angiogenin, an RNase-A-family protein, promotes angiogenesis and has been implicated in cancer, neurodegenerative diseases and epigenetic inheritance(1-10). After activation during cellular stress, angiogenin cleaves tRNAs at the anticodon loop, resulting in translation repression(11-15). However, the catalytic activity of isolated angiogenin is very low, and the mechanisms of the enzyme activation and tRNA specificity have remained a puzzle(3,16-23). Here we identify these mechanisms using biochemical assays and cryogenic electron microscopy (cryo-EM). Our study reveals that the cytosolic ribosome is the activator of angiogenin. A cryo-EM structure features angiogenin bound in the A site of the 80S ribosome. The C-terminal tail of angiogenin is rearranged by interactions with the ribosome to activate the RNase catalytic centre, making the enzyme several orders of magnitude more efficient in tRNA cleavage. Additional 80S-angiogenin structures capture how tRNA substrate is directed by the ribosome into angiogenin's active site, demonstrating that the ribosome acts as the specificity factor. Our findings therefore suggest that angiogenin is activated by ribosomes with a vacant A site, the abundance of which increases during cellular stress(24-27). These results may facilitate the development of therapeutics to treat cancer and neurodegenerative diseases. Structural mechanism of angiogenin activation by the ribosome.,Loveland AB, Koh CS, Ganesan R, Jacobson A, Korostelev AA Nature. 2024 Jun;630(8017):769-776. doi: 10.1038/s41586-024-07508-8. Epub 2024 , May 8. PMID:38718836 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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