9up6: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
Line 1: Line 1:
'''Unreleased structure'''


The entry 9up6 is ON HOLD  until Paper Publication
==Klebsiella pneumoniae NagA==
<StructureSection load='9up6' size='340' side='right'caption='[[9up6]], [[Resolution|resolution]] 3.67&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9up6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UP6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.67&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9up6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9up6 OCA], [https://pdbe.org/9up6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9up6 RCSB], [https://www.ebi.ac.uk/pdbsum/9up6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9up6 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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.


Authors:  
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<ref>PMID:40877019</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9up6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Lee SY]]
[[Category: Park HH]]
Retrieved from "https://proteopedia.org/9up6"