View source for 5tne


==Crystal structure of the E153Q mutant of the CFTR inhibitory factor Cif containing the adducted cis-Stilbene Oxide hydrolysis intermediate==
<StructureSection load='5tne' size='340' side='right'caption='[[5tne]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tne]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_UCBPP-PA14 Pseudomonas aeruginosa UCBPP-PA14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TNE 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7F6:(1~{R},2~{R})-1,2-diphenylethane-1,2-diol'>7F6</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=5tne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tne OCA], [https://pdbe.org/5tne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tne RCSB], [https://www.ebi.ac.uk/pdbsum/5tne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tne ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2ZD27_PSEAB A0A0H2ZD27_PSEAB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pseudomonas aeruginosa secretes an epoxide hydrolase with catalytic activity that triggers degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and perturbs other host defense networks. Targets of this CFTR inhibitory factor (Cif) are largely unknown, but include an epoxy-fatty acid. In this class of signaling molecules, chirality can be an important determinant of physiological output and potency. Here we explore the active-site chemistry of this two-step alpha/beta-hydrolase and its implications for an emerging class of virulence enzymes. In combination with hydrolysis data, crystal structures of 15 trapped hydroxyalkyl-enzyme intermediates reveal the stereochemical basis of Cif's substrate specificity, as well as its regioisomeric and enantiomeric preferences. The structures also reveal distinct sets of conformational changes that enable the active site to expand dramatically in two directions, accommodating a surprising array of potential physiological epoxide targets. These new substrates may contribute to Cif's diverse effects in vivo, and thus to the success of P. aeruginosa and other pathogens during infection.

Active-Site Flexibility and Substrate Specificity in a Bacterial Virulence Factor: Crystallographic Snapshots of an Epoxide Hydrolase.,Hvorecny KL, Bahl CD, Kitamura S, Lee KSS, Hammock BD, Morisseau C, Madden DR Structure. 2017 May 2;25(5):697-707.e4. doi: 10.1016/j.str.2017.03.002. Epub 2017, Apr 6. PMID:28392259<ref>PMID:28392259</ref>

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

==See Also==
*[[CFTR inhibitory factor|CFTR inhibitory factor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa UCBPP-PA14]]
[[Category: Hvorecny KL]]
[[Category: Madden DR]]