8peg

Escherichia coli paused disome complex (queueing 70S non-rotated closed PRE state)

spinqualitylabelsall models 8peg, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8peg is a 10 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: 12A, 1MG, 2MA, 2MG, 3TD, 4OC, 4SU, 5MC, 5MU, 6MZ, 7MG, ATP, CM0, G7M, H2U, MA6, MG, MIA, OMC, OMG, OMU, PSU, RSP, UR3, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL36_ECOLI Publication Abstract from PubMed Structural studies of translating ribosomes traditionally rely on in vitro assembly and stalling of ribosomes in defined states. To comprehensively visualize bacterial translation, we reactivated ex vivo-derived E. coli polysomes in the PURE in vitro translation system and analyzed the actively elongating polysomes by cryo-EM. We find that 31% of 70S ribosomes assemble into disome complexes that represent eight distinct functional states including decoding and termination intermediates, and a pre-nucleophilic attack state. The functional diversity of disome complexes together with RNase digest experiments suggests that paused disome complexes transiently form during ongoing elongation. Structural analysis revealed five disome interfaces between leading and queueing ribosomes that undergo rearrangements as the leading ribosome traverses through the elongation cycle. Our findings reveal at the molecular level how bL9's CTD obstructs the factor binding site of queueing ribosomes to thwart harmful collisions and illustrate how translation dynamics reshape inter-ribosomal contacts. Transient disome complex formation in native polysomes during ongoing protein synthesis captured by cryo-EM.,Flugel T, Schacherl M, Unbehaun A, Schroeer B, Dabrowski M, Burger J, Mielke T, Sprink T, Diebolder CA, Guillen Schlippe YV, Spahn CMT Nat Commun. 2024 Feb 26;15(1):1756. doi: 10.1038/s41467-024-46092-3. PMID:38409277 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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