Our latest work on the structure and function of the native Pyruvate Dehydrogenase Complex Core is now online, showing once again the power of our lab’s integrative approach!
Cryo-EM, macromolecular docking and molecular dynamics simulations are combined to provide insights into the PDHc core scaffold interfaces as well as dissect the residing transacetylase reaction.
Congrats to all co-authors for this phenomenal work, which you can now read in Nature Communications:
“Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction“

This research presents a fascinating structural analysis of the Pyruvate Dehydrogenase Complex (PDHc) core using Cryo-EM, macromolecular docking, and molecular dynamics simulations. The study provides valuable insights into the scaffold interfaces and the transacetylase reaction, shedding light on the molecular interactions that stabilize coenzyme A and position the lipoate. The integrative approach used here underscores the power of combining multiple techniques to unravel complex biological systems. A significant contribution to the field!
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