9oaa: Difference between revisions

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New page: '''Unreleased structure''' The entry 9oaa is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 9oaa is ON HOLD
==The structure of TdfH from Neisseria gonorrhoeae==
<StructureSection load='9oaa' size='340' side='right'caption='[[9oaa]], [[Resolution|resolution]] 3.67&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9oaa]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA_1090 Neisseria gonorrhoeae FA 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OAA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[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=CA:CALCIUM+ION'>CA</scene>, <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=9oaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9oaa OCA], [https://pdbe.org/9oaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9oaa RCSB], [https://www.ebi.ac.uk/pdbsum/9oaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9oaa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5F845_NEIG1 Q5F845_NEIG1]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
With an estimated 106 million global cases annually, Neisseria gonorrhoeae (Ngo) poses a significant public health problem. Ngo demonstrates a remarkable capacity to overcome nutritional immunity through the deployment of specialized transporters that pirate metals such as zinc from human proteins such as calprotectin (hCP). We report the cryo-EM structure of Ngo TdfH in complex with a heterotetramer of hCP. An extensive binding interface is mediated almost entirely by the S100A9 subunits of hCP. Mutagenesis studies of residues in the large binding interface reveal minimal effects from single-site mutations, whereas larger truncations disrupt binding and function. These results support a mechanistic model based on the large interaction interface overcoming a steric clash between alpha-helix III of S100A9 and loops 5 and 9 of TdfH, which leads to the distortion of the proximal His6 site, followed by zinc release, and import through the barrel domain.


Authors:  
Structural insights into zinc piracy by Neisseria gonorrhoeae to overcome nutritional immunity.,Gheinani PT, Bera A, Stoudenmire-Saylor J, Lien Y, Harrison SA, Criss A, Chazin WJ, Noinaj N, Cornelissen CN Structure. 2026 Feb 5;34(2):322-333.e6. doi: 10.1016/j.str.2025.11.014. Epub 2025 , Dec 18. PMID:41418777<ref>PMID:41418777</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 9oaa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Neisseria gonorrhoeae FA 1090]]
[[Category: Bera A]]
[[Category: Noinaj N]]
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