6sl9: Difference between revisions

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-'''Unreleased structure'''
-The entry 6sl9 is ON HOLD  until Paper Publication
+==High resolution apo structure of isomerase PaaG==
+<StructureSection load='6sl9' size='340' side='right'caption='[[6sl9]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6sl9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SL9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SL9 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6sl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sl9 OCA], [http://pdbe.org/6sl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sl9 RCSB], [http://www.ebi.ac.uk/pdbsum/6sl9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sl9 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Numerous aromatic compounds are aerobically degraded in bacteria via the central intermediate phenylacetic acid (paa). In one of the key steps of this widespread catabolic pathway, 1,2-epoxyphenylacetyl-CoA is converted by PaaG into the heterocyclic oxepin-CoA. PaaG thereby elegantly generates an alpha,beta-unsaturated CoA ester that is predisposed to undergo beta-oxidation subsequent to hydrolytic ring-cleavage. Moreover, oxepin-CoA serves as a precursor for secondary metabolites (e.g., tropodithietic acid) that act as antibiotics and quorum-sensing signals. Here we verify that PaaG adopts a second role in aromatic catabolism by converting cis-3,4-didehydroadipoyl-CoA into trans-2,3-didehydroadipoyl-CoA and corroborate a Delta(3),Delta(2)-enoyl-CoA isomerase-like proton shuttling mechanism for both distinct substrates. Biochemical and structural investigations of PaaG reveal active site adaptations to the structurally different substrates and provide detailed insight into catalysis and control of stereospecificity. This work elucidates the mechanism of action of unusual isomerase PaaG and sheds new light on the ubiquitous enoyl-CoA isomerases of the crotonase superfamily.
-Authors:
+Structural and Mechanistic Basis of an Oxepin-CoA Forming Isomerase in Bacterial Primary and Secondary Metabolism.,Spieker M, Saleem-Batcha R, Teufel R ACS Chem Biol. 2019 Nov 18. doi: 10.1021/acschembio.9b00742. PMID:31689071<ref>PMID:31689071</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6sl9" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saleem-Batcha, R]]
+[[Category: Spieker, M]]
+[[Category: Teufel, R]]
+[[Category: Crotonase]]
+[[Category: Isomerase]]
+[[Category: Phenylacetic acid catabolism]]
+[[Category: Tropodithietic acid]]