A look into DGAT1 through the EM lenses

With the advent of modern detectors and robust structure solution pipeline, cryogenic electron microscopy has recently proved to be game changer in structural biology. Membrane proteins are challenging targets for structural biologists. This minireview focuses a membrane embedded triglyceride synthesizing machine, DGAT1. Decades of research had built the foundational knowledge on this enzyme's activity. However, recently solved cryo-EM structures of this enzyme, in apo and bound form, has provided critical mechanistic insights. The flipping of the catalytic histidine is critical of enzyme catalysis. The structures explain why the enzyme has preference to long fatty acyl chains over the short forms.

Automated summary

With the help of modern detectors and robust structure solution pipeline, cryogenic electron microscopy has brought significant changes to the field of structural biology. Membrane proteins, a challenging target, have received much attention. This minireview focuses on DGAT1, a membrane embedded triglyceride synthesizing machine. Recent cryo-EM structures of this enzyme have provided valuable insights into its mechanism, including the role of the flipping of catalytic histidine and the preference for long fatty acyl chains.