Structural Basis for Tetramerization of <i>Klebsiella pneumoniae</i> <i>N</i>-Acetylglucosamine-6-Phosphate Deacetylase.

ABSTRACT: N-acetylglucosamine-6-phosphate deacetylase (NagA) is a conserved enzyme involved in bacterial amino sugar metabolism, catalyzing the conversion of GlcNAc-6-phosphate to GlcN-6-phosphate and acetate. While NagA typically function as dimers, its quaternary diversity across species remains underexplored. Here, we present the crystal structure of Klebsiella pneumoniae (kpNagA), which forms a homotetrameric assembly both in crystal and in solution, as confirmed by SEC-MALS. Each monomer adopts a canonical (β/α)₈ TIM barrel fold with a β-sandwich subdomain, and its active site, located around β10-β11 and α3-α4, coordinates a divalent zinc ion. Comparative analyses revealed conserved dimer interfaces but divergent tetrameric arrangements. Notably, Pasteurella multocida N

SUBMITTER: Lee SY 

PROVIDER: S-EPMC12409433 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature