View source for 9psd


==High-resolution crystal structure of Vibrio cholerae NFeoB bound to GDP-AlF3==
<StructureSection load='9psd' size='340' side='right'caption='[[9psd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9psd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9PSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PSD 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9psd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9psd OCA], [https://pdbe.org/9psd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9psd RCSB], [https://www.ebi.ac.uk/pdbsum/9psd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9psd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A655NVH2_VIBCL A0A655NVH2_VIBCL] Probable transporter of a GTP-driven Fe(2+) uptake system.[RuleBase:RU362098]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The acquisition of iron is critical for the survival and the virulence of numerous infectious pathogens, and most bacteria acquire ferrous iron (Fe(2+)) by utilizing the ferrous iron transport (Feo) system. FeoB is the main component of this system and its function is regulated by its soluble cytosolic domain, termed NFeoB. We have recently begun to define the structure and the mechanism of the Feo system from the bacterium Vibrio cholerae, the causative agent of the disease cholera. However, major structural gaps in our understanding of the nucleotide-promiscuous V. cholerae NFeoB still exist. In this work, we have determined several new X-ray crystal structures that reveal distinct snapshots of the VcNFeoB domain in uncommon and unprecedented states, ultimately illuminating the full catalytic cycle of this NTPase. This work reveals important functional features of VcNFeoB that may be leveraged and ultimately targeted to prevent the infectivity and the spread of cholera.

The Structure of the Full Catalytic Cycle of Vibrio cholerae NFeoB.,Magante K, Armstrong CM, Lee M, Smith AT J Mol Biol. 2026 May 1;438(9):169727. doi: 10.1016/j.jmb.2026.169727. Epub 2026 , Feb 20. PMID:41724262<ref>PMID:41724262</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9psd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Lee M]]
[[Category: Magante K]]
[[Category: Smith AT]]