View source for 5nr2


==Crystal structure of the ferric enterobactin receptor (PfeA) from Pseudomonas aeruginosa in complex with azotochelin==
<StructureSection load='5nr2' size='340' side='right'caption='[[5nr2]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nr2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NR2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=95B:Azotochelin'>95B</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pfeA, PA2688 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nr2 OCA], [http://pdbe.org/5nr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nr2 RCSB], [http://www.ebi.ac.uk/pdbsum/5nr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nr2 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PFEA_PSEAE PFEA_PSEAE]] Specific receptor for the siderophore ferric enterobactin. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteria use small molecules called siderophores to scavenge iron. Siderophore-Fe(3+) complexes are recognised by outer-membrane transporters and imported into the periplasm in a process dependent on the inner-membrane protein TonB. The siderophore enterobactin is secreted by members of the family Enterobacteriaceae, but many other bacteria including Pseudomonas species can use it. Here, we show that the Pseudomonas transporter PfeA recognises enterobactin using extracellular loops distant from the pore. The relevance of this site is supported by in vivo and in vitro analyses. We suggest there is a second binding site deeper inside the structure and propose that correlated changes in hydrogen bonds link binding-induced structural re-arrangements to the structural adjustment of the periplasmic TonB-binding motif.

The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model.,Moynie L, Milenkovic S, Mislin GLA, Gasser V, Malloci G, Baco E, McCaughan RP, Page MGP, Schalk IJ, Ceccarelli M, Naismith JH Nat Commun. 2019 Aug 14;10(1):3673. doi: 10.1038/s41467-019-11508-y. PMID:31413254<ref>PMID:31413254</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nr2" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ferric enterobactin receptor|Ferric enterobactin receptor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseae]]
[[Category: Moynie, L]]
[[Category: Naismith, J H]]
[[Category: Azotochelin]]
[[Category: Membrane protein]]
[[Category: Outer membrane receptor]]
[[Category: Pa2688]]
[[Category: Pfea]]