Molecular Mechanisms Underlying the Loop-Closing Dynamics of β-1,4 Galactosyltransferase 1.

ABSTRACT: The β-1,4 galactosylation catalyzed by β-1,4 galactosyltransferases (β4Gal-Ts) is not only closely associated with diverse physiological and pathological processes in humans but also widely applied in the N-glycan modification of protein glycoengineering. The loop-closing process of β4Gal-Ts is an essential intermediate step intervening in the binding events of donor substrate (UDP-Gal/Mn²⁺) and acceptor substrate during its catalytic cycle, with a significant impact on the galactosylation activities. However, the molecular mechanisms in regulating loop-closing dynamics are not entirely clear. Here, we construct Markov state models (MSMs) based on approximately 20 μs of all-atom molecular dynamics simulations to explore the loop-closing dynamics for β-1,4 galactosyltransf

SUBMITTER: Tian J 

PROVIDER: S-EPMC11734692 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature