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Structure of an archaeal ribosome reveals a divergent active site and hibernation factor (Nat Microbiol, 2025)

By Amos Nissley

C-GEM researchers identified archaeal ribosomes with highly divergent peptidyl transferase centers (PTC). Cryo-EM structures of the Pyrobaculum calidifontis ribosome revealed that unique archaeal ribosomal protein (rProtein) sequences reorganize the PTC, enabling rRNA sequence variation. Modifying E. coli rProteins to resemble those in archaea enabled E. coli ribosomes to better accommodate PTC sequence variation. These findings demonstrate the role of rProteins in tuning the mutational robustness of the PTC and provide new design principles for future ribosome engineering efforts. 

This work involved contributions from the Cate lab and C-GEM collaborator Professor Jill Banfield.

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