Allosteric regulation of the ribosomal A site revealed by molecular dynamics simulationsстатья
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Дата последнего поиска статьи во внешних источниках: 6 февраля 2020 г.
Аннотация:The A site of the ribosome, which determines binding and orientation of a new amino acid residue for the peptidyl transferase reaction, was found to occupy two different conformational states upon the molecular dynamics (MD) simulations study of the 70S E. coli ribosome. One of the states, defined as “inactive”, appeared in trajectories with E–tRNA, mutations A2531U and UU2492–3C, which are known to decrease the A site affinity to the tRNA. This conformational transition was found to be allosterically connected with conformational alterations in different sites of the macromolecular complex, including the E site of the ribosome and intersubunit bridge B7a located near the E site.
The MD simulations of the ribosomes with the A2531U and UU2492–3C mutations known to decrease the A–tRNA retention in the ribosome, demonstrated partial switching of the 16S and 23S rRNA conformation towards its characteristic one in the P/P, E/E state.