I especially thank Balázs Fábián in @hummerlab.bsky.social for leading the MD simulations, and Hartmut Michel (@mpibp.bsky.social), Schara Safarian and Etana Padan for their guidance, as well as @sonjawelsch.bsky.social and the cryo-EM facility team!
Together with the Hurt lab and @beckmannlab.bsky.social , we uncovered that Rrp12 coordinates ordered decoding center assembly. Wrongly assembled DC triggers premature recruitment of Rio1 in the nucleoplasm most likely for quality control. #ribosome #cryo-EM
I've written a review on what I think is an extremely exciting direction in cryo-EM:
Cryo-EM of endogenous membrane proteins in their native lipid bilayer
Open access in Quarterly Reviews of Biophysics:
doi.org/10.1017/S003...
SNDing proteins into the membrane! Our new publication from @melaniemcdowell.bsky.social ’s group identifies the SND3 protein as a new route for membrane protein insertion! 🍄 📘 Read more here: www.mpg.de/25599408/102... Image: Louise Duever.
We also captured a Na⁺-bound state.
The ion sits between Asp163, Asp164, Thr132, and water—giving a clear picture of how NhaA recognizes its substrate.
One of the surprises: we can now see the N-terminal tail.
It acts like a plug at the cytoplasmic entrance—blocking access at low pH and moving away as pH increases.
Together, these data link pH sensing, ion binding, and N-terminal dynamics in NhaA, providing a structural framework for understanding Na⁺/H⁺ antiporters.
Simulations reveal what happens next:
Na⁺ binding triggers stepwise deprotonation—first Asp164, then Asp163—supporting a two-aspartate mechanism.
Prof. Hartmut Michel's group @mpibp.bsky.social is recruiting a postdoc in structural bioenergetics. See the link for more detail.👇
It's finally out now in @natcomms.nature.com!
We used cryo-EM + simulations to watch the Na⁺/H⁺ antiporter NhaA in action across a wide range of pH—and uncover how pH, Na⁺ binding, and structural changes are coupled.
Read here 🔗 www.nature.com/articles/s41...