6nsh | pdb_00006nsh

Modified ASL proline bound to Thermus thermophilus 70S (near-cognate)

spinqualitylabelsall models 6nsh, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nsh is a 20 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.397Å Ligands: 1MG, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL2_THET8 One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial (By similarity). Makes several contacts with the 16S rRNA (forming bridge B7b) in the 70S ribosome.[HAMAP-Rule:MF_01320_B] Publication Abstract from PubMed Modifications in the tRNA anticodon loop, adjacent to the three-nucleotide anticodon, influence translation fidelity by stabilizing the tRNA to allow for accurate reading of the mRNA genetic code. One example is the N1-methylguaonosine modification at guanine nucleotide 37 (m(1)G37) located in the anticodon loop, immediately adjacent to the anticodon nucleotides 34-36. The absence of m(1)G37 in tRNA(Pro) causes +1 frameshifting on polynucleotide, slippery codons. Here, we report structures of the bacterial ribosome containing tRNA(Pro) bound to either cognate or slippery codons to determine how the m(1)G37 modification prevents mRNA frameshifting. The structures reveal that certain codon-anticodon contexts and m(1)G37 destabilize interactions of tRNA(Pro) with the peptidyl site, causing large conformational changes typically only seen during EF-G mediated translocation of the mRNA-tRNA pairs. These studies provide molecular insights into how m(1)G37 stabilizes the interactions of tRNA(Pro) with the ribosome and the influence of slippery codons on the mRNA reading frame. Structural insights into mRNA reading frame regulation by tRNA modification and slippery codon-anticodon pairing.,Hoffer E, Hong S, Sunita S, Maehigashi T, Gonzalez RL Jnr, Whitford P, Dunham CM Elife. 2020 Oct 5;9. pii: 51898. doi: 10.7554/eLife.51898. PMID:33016876 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein THX 3D structures

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