<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Lee SY</submitter><funding>Ministry of Science and ICT, South Korea</funding><funding>National Research Foundation of Korea</funding><pagination>e2505019</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12409433</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>35</volume><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 &lt;i>Klebsiella pneumoniae&lt;/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)&lt;sub>8&lt;/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, &lt;i>Pasteurella multocida&lt;/i> N</pubmed_abstract><journal>Journal of microbiology and biotechnology</journal><pubmed_title>Structural Basis for Tetramerization of &amp;lt;i&amp;gt;Klebsiella pneumoniae&amp;lt;/i&amp;gt; &amp;lt;i&amp;gt;N&amp;lt;/i&amp;gt;-Acetylglucosamine-6-Phosphate Deacetylase.</pubmed_title><pmcid>PMC12409433</pmcid><funding_grant_id>RS-2025-02316334</funding_grant_id><pubmed_authors>Lee SY</pubmed_authors><pubmed_authors>Park HH</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structural Basis for Tetramerization of &amp;lt;i&amp;gt;Klebsiella pneumoniae&amp;lt;/i&amp;gt; &amp;lt;i&amp;gt;N&amp;lt;/i&amp;gt;-Acetylglucosamine-6-Phosphate Deacetylase.</name><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 &lt;i>Klebsiella pneumoniae&lt;/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)&lt;sub>8&lt;/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, &lt;i>Pasteurella multocida&lt;/i> N</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Aug</publication><modification>2026-05-29T21:41:28.471Z</modification><creation>2026-04-08T06:06:11.965Z</creation></dates><accession>S-EPMC12409433</accession><cross_references><pubmed>40877019</pubmed><doi>10.4014/jmb.2505.05019</doi></cross_references></HashMap>