7ls2

80S ribosome from mouse bound to eEF2 (Class I)

spinqualitylabelsall models 7ls2, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ls2 is a 10 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.1Å Ligands: 1MA, 2MG, 4AC, 5MC, 6MZ, A2M, B8N, B8Q, B8T, B8W, B9B, B9H, DDE, E6G, E7G, G7M, GDP, I4U, MG, MHG, MLZ, OMC, OMG, OMU, P7G, PSU, UR3, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL7_MOUSE Component of the large ribosomal subunit (By similarity). Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs (By similarity).[UniProtKB:P18124] Publication Abstract from PubMed Processing bodies (p-bodies) are a prototypical phase-separated RNA-containing granule. Their abundance is highly dynamic and has been linked to translation. Yet, the molecular mechanisms responsible for coordinate control of the two processes are unclear. Here, we uncover key roles for eEF2 kinase (eEF2K) in the control of ribosome availability and p-body abundance. eEF2K acts on a sole known substrate, eEF2, to inhibit translation. We find that the eEF2K agonist nelfinavir abolishes p-bodies in sensory neurons and impairs translation. To probe the latter, we used cryo-electron microscopy. Nelfinavir stabilizes vacant 80S ribosomes. They contain SERBP1 in place of mRNA and eEF2 in the acceptor site. Phosphorylated eEF2 associates with inactive ribosomes that resist splitting in vitro. Collectively, the data suggest that eEF2K defines a population of inactive ribosomes resistant to recycling and protected from degradation. Thus, eEF2K activity is central to both p-body abundance and ribosome availability in sensory neurons. Functionally distinct roles for eEF2K in the control of ribosome availability and p-body abundance.,Smith PR, Loerch S, Kunder N, Stanowick AD, Lou TF, Campbell ZT Nat Commun. 2021 Nov 23;12(1):6789. doi: 10.1038/s41467-021-27160-4. PMID:34815424 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures Ribosome 3D structures 3D sructureseceptor for activated protein kinase C 1

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