Structural basis of collagen glucosyltransferase function and its serendipitous role in kojibiose synthesis.

ABSTRACT: Collagen glucosyltransferases catalyze a unique type of collagen glucosylation that is critical for biological processes and disease mechanisms. However, the structural regulation of collagen glucosyltransferases remains poorly understood. Here, we report the crystal structures of a mimiviral collagen glucosyltransferase in its apo form and in complexes with uridine diphosphate (UDP) and the disaccharide product. Our findings reveal that the enzyme functions as a homodimer, stabilized by a loop from one subunit locking into a cleft on the opposite subunit. This dimerization enables UDP-glucose binding cooperativity and enzymatic activity, a property conserved in the human homolog. Further structural analyses suggest an induced fit model for UDP interaction, mediated by Lysine 222. The dime

SUBMITTER: Kim JS 

PROVIDER: S-EPMC11838735 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature