9up6 | pdb_00009up6

Klebsiella pneumoniae NagA

spinqualitylabelsall models 9up6, resolution 3.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9up6 is a 8 chain structure with sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.67Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 (beta/alpha)(8) TIM barrel fold with a beta-sandwich subdomain, and its active site, located around beta10-beta11 and alpha3-alpha4, coordinates a divalent zinc ion. Comparative analyses revealed conserved dimer interfaces but divergent tetrameric arrangements. Notably, Pasteurella multocida 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. Structural Basis for Tetramerization of Klebsiella pneumoniae N-Acetylglucosamine-6-Phosphate Deacetylase.,Lee SY, Park HH J Microbiol Biotechnol. 2025 Aug 26;35:e2505019. doi: 10.4014/jmb.2505.05019. PMID:40877019 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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