{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lee SY"],"funding":["Ministry of Science and ICT, South Korea","National Research Foundation of Korea"],"pagination":["e2505019"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12409433"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["35"],"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 <i>Klebsiella pneumoniae</i> (kpNagA), which forms a homotetrameric assembly both in crystal and in solution, as confirmed by SEC-MALS. Each monomer adopts a canonical (β/α)<sub>8</sub> 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, <i>Pasteurella multocida</i> N"],"journal":["Journal of microbiology and biotechnology"],"pubmed_title":["Structural Basis for Tetramerization of &lt;i&gt;Klebsiella pneumoniae&lt;/i&gt; &lt;i&gt;N&lt;/i&gt;-Acetylglucosamine-6-Phosphate Deacetylase."],"pmcid":["PMC12409433"],"funding_grant_id":["RS-2025-02316334"],"pubmed_authors":["Lee SY","Park HH"],"additional_accession":[]},"is_claimable":false,"name":"Structural Basis for Tetramerization of &lt;i&gt;Klebsiella pneumoniae&lt;/i&gt; &lt;i&gt;N&lt;/i&gt;-Acetylglucosamine-6-Phosphate Deacetylase.","description":"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 <i>Klebsiella pneumoniae</i> (kpNagA), which forms a homotetrameric assembly both in crystal and in solution, as confirmed by SEC-MALS. Each monomer adopts a canonical (β/α)<sub>8</sub> 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, <i>Pasteurella multocida</i> N","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-29T21:41:28.471Z","creation":"2026-04-08T06:06:11.965Z"},"accession":"S-EPMC12409433","cross_references":{"pubmed":["40877019"],"doi":["10.4014/jmb.2505.05019"]}}