EngA adopts multiple distinct conformational states during ribosome assembly

Cryo-EM structures of Mycobacterium smegmatis 50S with EngA-bound GTPγS or GDP (2.8–3.5 Å) reveal coordinated rearrangements and an SLJ assembly intermediate.

• Why it matters: The mechanism by which EngA’s GTP hydrolysis supports late 50S maturation is poorly defined, especially for EngA-bound GDP states.
• What they did: The authors determined cryo-EM structures of 50S–EngA complexes with EngA-bound GTPγS or GDP, then analyzed coordinated structural changes and intermediate formation.
• The result: EngA-bound GDP adopts distinct conformations in ribosome-bound versus unbound states, enabling a multi-state conformational model for EngA-assisted ribosome assembly.

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