View source for 6wef


==Copper-bound D92H variant of Campylobacter jejuni P19==
<StructureSection load='6wef' size='340' side='right'caption='[[6wef]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6wef]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_81-176 Campylobacter jejuni subsp. jejuni 81-176]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WEF 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]] 2.501&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6wef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wef OCA], [https://pdbe.org/6wef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wef RCSB], [https://www.ebi.ac.uk/pdbsum/6wef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wef ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H3PA01_CAMJJ A0A0H3PA01_CAMJJ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Campylobacter jejuni is a leading cause of food-borne gastrointestinal disease in humans and uropathogenic Escherichia coli is a leading cause of urinary tract infections. Both human pathogens harbour a homologous iron uptake system (termed cjFetM-P19 in C. jejuni and ecFetM-FetP in E. coli). Although these systems are important for growth under iron limitation, the mechanisms by which these systems function during iron transport remain undefined. The copper ions bound to P19 and FetP, the homologous periplasmic proteins, are coordinated in an uncommon penta-dentate manner involving a Met-Glu-His3 motif and exhibit positional plasticity. Here we demonstrate the function of the Met and Glu residues in modulating copper binding and controlling copper positioning through site-directed variants, binding assays, and crystal structures. Growth of C. jejuni strains with these p19 variants is impaired under iron limited conditions as compared to the wild-type strain. Additionally, an acidic residue-rich secondary site is required for binding iron and function in vivo. Finally, western blot analyses demonstrate direct and specific interactions between periplasmic P19 and FetP with the large periplasmic domain of their respective inner membrane transporters cjFetM and ecFetM.

A copper site is required for iron transport by the periplasmic proteins P19 and FetP.,Chan ACK, Lin H, Koch D, Grass G, Nies DH, Murphy MEP Metallomics. 2020 Oct 21;12(10):1530-1541. doi: 10.1039/d0mt00130a. PMID:32780051<ref>PMID:32780051</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wef" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Campylobacter jejuni subsp. jejuni 81-176]]
[[Category: Large Structures]]
[[Category: Chan AC]]
[[Category: Murphy ME]]