9xwo

Cryo-EM structure of SecM-arrested 70S ribosome (short SecM)

spinqualitylabelsall models 9xwo, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9xwo 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 2.89Å Ligands: 1MG, 2MA, 2MG, 3TD, 4D4, 4OC, 4SU, 5MC, 5MU, 6MZ, CM0, D2T, G7M, H2U, IAS, K, MA6, MEQ, MG, MS6, OMC, OMG, OMU, PRO, PSU, SPD, UR3, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RS2_ECOLI Publication Abstract from PubMed ATP-binding cassette subfamily F (ABCF) proteins interact with the ribosome to resolve translation defects near the peptidyl transferase center (PTC). In Escherichia coli, four ABCF proteins (EttA, Uup, YbiT, and YheS) selectively promote translation of distinct problematic nascent peptide sequences, but their molecular mechanisms remain unclear. Here, we present a 2.8 A cryo-EM structure of the ribosome in complex with an ATPase-deficient mutant of YheS and investigate how it releases ribosomes arrested by the SecM nascent chain. YheS binds to the ribosomal E-site via the L1 stalk, and its P-site tRNA-interaction motif (PtIM) extends toward the PTC, displacing the CCA end of the P-site tRNA. Notably, the cryo-EM density corresponding to the SecM nascent chain within the exit tunnel is largely lost upon YheS binding. These observations suggest that YheS relieves peptide sequence-dependent stalling by perturbing nascent chain-tunnel interactions through P-site tRNA relocation. Steered molecular dynamics simulations provide qualitative support for this model. Together, our findings provide mechanistic insight into a mode of arrest release distinct from the translocon-mediated release mechanism. Structural insights into YheS-mediated release of SecM-arrested ribosome.,Iso K, Ikeda T, Yamasaki K, Ando Y, Sano FK, Furuta T, Taguchi H, Nureki O, Chadani Y, Itoh Y Nat Commun. 2026 Jun 9;17(1):4963. doi: 10.1038/s41467-026-72863-1. PMID:42265116 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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