9UP6

Klebsiella pneumoniae NagA

Summary for 9UP6

• Entry DOI: 10.2210/pdb9up6/pdb
• Descriptor: N-acetylglucosamine-6-phosphate deacetylase, ZINC ION (2 entities in total)
• Functional Keywords: deacetylase, hydrolase, carbohydrate metabolism, n-acetylglucosamine-6-phosphate catabolism
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 8
• Total formula weight: 332230.11

Authors

Lee, S.Y.,Park, H.H. (deposition date: 2025-04-27, release date: 2026-03-04)

Primary citation

Lee, S.Y.,Park, H.H.
Structural Basis for Tetramerization of Klebsiella pneumoniae N -Acetylglucosamine-6-Phosphate Deacetylase.
J Microbiol Biotechnol., 35:e2505019-e2505019, 2025

PubMed 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 (kpNagA), which forms a homotetrameric assembly both in crystal and in solution, as confirmed by SEC-MALS. Each monomer adopts a canonical (β/α) 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, NagA also forms a stable tetramer, albeit via a distinct interface. These findings suggest species-specific tetramerization and broaden our understanding of NagA structural diversity and potential antibiotic targets.

PubMed: 40877019
DOI: 10.4014/jmb.2505.05019

Experimental method

X-RAY DIFFRACTION (3.67 Å)