5np6 | pdb_00005np6

70S structure prior to bypassing

Loading... Status: waiting for Mol* initialization Structural highlights 5np6 is a 10 chain structure with sequence from Escherichia coli, Escherichia coli K-12 and Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.6Å Ligands: 1MG, 2MA, 2MG, 3TD, 4OC, 5MC, 5MU, 6MZ, 7MG, H2U, MA6, OMC, OMG, OMU, PSU, UR3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TOPS_BPT4 Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. T4 topoisomerase makes double-strand breaks. Publication Abstract from PubMed Bypassing is a recoding event that leads to the translation of two distal open reading frames into a single polypeptide chain. We present the structure of a translating ribosome stalled at the bypassing take-off site of gene 60 of bacteriophage T4. The nascent peptide in the exit tunnel anchors the P-site peptidyl-tRNAGly to the ribosome and locks an inactive conformation of the peptidyl transferase center (PTC). The mRNA forms a short dynamic hairpin in the decoding site. The ribosomal subunits adopt a rolling conformation in which the rotation of the small subunit around its long axis causes the opening of the A-site region. Together, PTC conformation and mRNA structure safeguard against premature termination and read-through of the stop codon and reconfigure the ribosome to a state poised for take-off and sliding along the noncoding mRNA gap. Ribosome rearrangements at the onset of translational bypassing.,Agirrezabala X, Samatova E, Klimova M, Zamora M, Gil-Carton D, Rodnina MV, Valle M Sci Adv. 2017 Jun 7;3(6):e1700147. doi: 10.1126/sciadv.1700147. eCollection 2017 , Jun. PMID:28630923 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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