Luigi Scietti
@luigiscietti.bsky.social
Scientist interested in #proteinexpression, #biochemistry, #biophysics and #structuralbiology (X-ray crystallography and #cryoEM)
coordinator of the biochemistry and structural biology unit at the European Institute of Oncology (IEO)
coordinator of the biochemistry and structural biology unit at the European Institute of Oncology (IEO)
I also had fun in making gummy GLT25D1 making #notthecover using #blender
April 22, 2025 at 9:34 AM
I also had fun in making gummy GLT25D1 making #notthecover using #blender
This was a massive work from @fornerislab.bsky.social fellows to ehihc I contributed when I was Postdoc, and great #teamwork with Giorgio Colombo lab, @claudio-iacobucci.bsky.social and Alberta Pinnola lab.
April 22, 2025 at 9:34 AM
This was a massive work from @fornerislab.bsky.social fellows to ehihc I contributed when I was Postdoc, and great #teamwork with Giorgio Colombo lab, @claudio-iacobucci.bsky.social and Alberta Pinnola lab.
we found that the GT1 domain, while not catalytic, is surprisingly capable of binding Ca²⁺ and UDP-α-galactose. This was intriguing to us, but all the mutants in the GT1 site did not produce folded protein, consistent with a structural role for the GT1 (also confirmed by MD).
April 22, 2025 at 9:34 AM
we found that the GT1 domain, while not catalytic, is surprisingly capable of binding Ca²⁺ and UDP-α-galactose. This was intriguing to us, but all the mutants in the GT1 site did not produce folded protein, consistent with a structural role for the GT1 (also confirmed by MD).
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.
April 22, 2025 at 9:34 AM
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.
April 22, 2025 at 9:34 AM
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
April 22, 2025 at 9:34 AM
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
Collagen's function are ensured by essential post-translational modifications including galactosylation.
GLT25D1 is the galactosyltransferase enzyme responsible for initiating the glycosylation of hydroxylysine in collagen. but its structure was missing until now
GLT25D1 is the galactosyltransferase enzyme responsible for initiating the glycosylation of hydroxylysine in collagen. but its structure was missing until now
April 22, 2025 at 9:34 AM
Collagen's function are ensured by essential post-translational modifications including galactosylation.
GLT25D1 is the galactosyltransferase enzyme responsible for initiating the glycosylation of hydroxylysine in collagen. but its structure was missing until now
GLT25D1 is the galactosyltransferase enzyme responsible for initiating the glycosylation of hydroxylysine in collagen. but its structure was missing until now