Amazing #cryoEM structures and incredible community here at @cniostopcancer.bsky.social for the “machines acting on DNA and RNA” congress!

I also had fun in making gummy GLT25D1 making #notthecover using #blender

And here the question: are they both active? which one is the responsible for the GalT activity? We combined #mutagenesis with #biophysics and #moleculardynamics to show that only the GT2 domain exhibits catalytic activity, facilitated by an unusual Glu-Asp-Asp motif critical for Mn²⁺ binding.

Each monomer contains two domains (GT1 and GT2) connected by a long but ordered linker. Surprisingly, both domains are capable of binding metal ions and the donor substrate UDP-α-galactose.

We solved the #Xray structure of GLT25D1/COLGALT1 via experimental phasing (yes, it was before #Alphafold) showing that it forms an elongated head-to-head homodimer