Computational characterization of the xanthan gum glycosyltransferase GumK.

ABSTRACT: The activity of GT-B glycosyltransferases (GTs) depends on their conformational flexibility and high substrate specificity, but the molecular basis of these features is still not well defined. The GT70 family contains a single well-characterized enzyme, GumK, a glucuronosyltransferase from Xanthomonas campestris required for xanthan gum biosynthesis. Here, we applied multiscale molecular simulations and sequence analysis to probe GumK dynamics and substrate specificity. We show that GumK undergoes twisting and bending motions constrained by interdomain contacts and modulated by membrane anchoring. Acceptor-substrate binding within an amphiphilic clamp promotes opening, whereas donor-substrate binding stabilizes closure, defining a substrate-dependent catalytic cycle. Specificity for UDP-gl

SUBMITTER: Luciano D 

PROVIDER: S-EPMC12768416 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature