Open AccessStructural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis
Author(s) -
Giuseppe Cimicata,
G. Fridkin,
Tanaya Bose,
Zohar Eyal,
Y. Halfon,
Elinor Breiner-Goldstein,
Tara Fox,
Ella Zimmerman,
Anat Bashan,
Natalia de Val,
Alexander Wlodawer,
Ada Yonath
Publication year - 2022
Publication title -
mbio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.562
H-Index - 121
eISSN - 2161-2129
pISSN - 2150-7511
DOI - 10.1128/mbio.00306-22
Subject(s) - ribosome , eukaryotic ribosome , protein biosynthesis , ribosomal rna , peptidyl transferase , biology , microbiology and biotechnology , rna , helix (gastropod) , biophysics , translation (biology) , ribosomal protein , biochemistry , protein subunit , chemistry , messenger rna , gene , ecology , snail
The mechanism that regulates the translocation step in ribosomes during protein synthesis is not fully understood. In this work, cryo-EM techniques used to image ribosomes fromStaphylococcus aureus after incubation at physiological temperature allowed the identification of a conformation of the helix 68 that has never been observed so far.