5tnh: Difference between revisions
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<StructureSection load='5tnh' size='340' side='right' caption='[[5tnh]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5tnh' size='340' side='right' caption='[[5tnh]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5tnh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TNH FirstGlance]. <br> | <table><tr><td colspan='2'>[[5tnh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseab Pseab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TNH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MS:(5Z,8Z,11Z,14Z,17R,18R)-17,18-dihydroxyicosa-5,8,11,14-tetraenoic+acid'>7MS</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MS:(5Z,8Z,11Z,14Z,17R,18R)-17,18-dihydroxyicosa-5,8,11,14-tetraenoic+acid'>7MS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kd2|3kd2]], [[4dmc|4dmc]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA14_26090 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208963 PSEAB])</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=5tnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnh OCA], [http://pdbe.org/5tnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tnh RCSB], [http://www.ebi.ac.uk/pdbsum/5tnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tnh ProSAT]</span></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=5tnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnh OCA], [http://pdbe.org/5tnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tnh RCSB], [http://www.ebi.ac.uk/pdbsum/5tnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tnh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Pseab]] | |||
[[Category: Hvorecny, K L]] | [[Category: Hvorecny, K L]] | ||
[[Category: Madden, D R]] | [[Category: Madden, D R]] | ||
Revision as of 13:17, 22 November 2017
Crystal structure of the E153Q mutant of the CFTR inhibitory factor Cif containing the adducted 17,18-EpETE hydrolysis intermediateCrystal structure of the E153Q mutant of the CFTR inhibitory factor Cif containing the adducted 17,18-EpETE hydrolysis intermediate
Structural highlights
Publication Abstract from PubMedPseudomonas 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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