Computational modeling of the molecular basis for the calcium-dependence of the mannuronan C-5 epimerase AvAlgE6 from Azotobacter vinelandii.

ABSTRACT: The mannuronan C-5 epimerases catalyze epimerization of β-d-mannuronic acid to α-l-guluronic acid in alginate polymers. The seven extracellular Azotobacter vinelandii epimerases (AvAlgE1-7) are calcium-dependent, and calcium is essential for the structural integrity of their carbohydrate binding R-modules. Ca²⁺ is also found in the crystal structures of the A-modules, where it is suggested to play a structural role. In this study, the structure of the catalytic A-module of the A. vinelandii mannuronan C-5 epimerase AvAlgE6 is used to investigate the role of this Ca²⁺. Molecular dynamics (MD) simulations with and without calcium reveal the possible importance of the bound Ca²⁺ in the hydrophobic packing of β-sheets. In addition, a putative calc

SUBMITTER: Gaardlos M 

PROVIDER: S-EPMC10066508 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature