2MER
Structure of helix 69 from escherichia coli 23s ribosomal rna
Summary for 2MER
Entry DOI | 10.2210/pdb2mer/pdb |
NMR Information | BMRB: 18974 |
Descriptor | RNA_(5'-R(P*GP*GP*CP*CP*GP*(PSU)P*AP*AP*CP*(PSU)P*AP*(PSU)P*AP*AP*CP*GP*GP*UP*C)-3') (1 entity in total) |
Functional Keywords | pseudouridine, helix 69, ribosomal, rna |
Total number of polymer chains | 1 |
Total formula weight | 6077.67 |
Authors | Jiang, J.,Aduri, R.,Chow, C.S.,Santalucia, J. (deposition date: 2013-09-26, release date: 2014-01-01, Last modification date: 2024-05-01) |
Primary citation | Jiang, J.,Aduri, R.,Chow, C.S.,Santalucia, J. Structure modulation of helix 69 from Escherichia coli 23S ribosomal RNA by pseudouridylations. Nucleic Acids Res., 42:3971-3981, 2014 Cited by PubMed Abstract: Helix 69 (H69) is a 19-nt stem-loop region from the large subunit ribosomal RNA. Three pseudouridine (Ψ) modifications clustered in H69 are conserved across phylogeny and known to affect ribosome function. To explore the effects of Ψ on the conformations of Escherichia coli H69 in solution, nuclear magnetic resonance spectroscopy was used to reveal the structural differences between H69 with (ΨΨΨ) and without (UUU) Ψ modifications. Comparison of the two structures shows that H69 ΨΨΨ has the following unique features: (i) the loop region is closed by a Watson-Crick base pair between Ψ1911 and A1919, which is potentially reinforced by interactions involving Ψ1911N1H and (ii) Ψ modifications at loop residues 1915 and 1917 promote base stacking from Ψ1915 to A1918. In contrast, the H69 UUU loop region, which lacks Ψ modifications, is less organized. Structure modulation by Ψ leads to alteration in conformational behavior of the 5' half of the H69 loop region, observed as broadening of C1914 non-exchangeable base proton resonances in the H69 ΨΨΨ nuclear magnetic resonance spectra, and plays an important biological role in establishing the ribosomal intersubunit bridge B2a and mediating translational fidelity. PubMed: 24371282DOI: 10.1093/nar/gkt1329 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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