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==The complex structure of pOPH S172C with ligand, ACA== | ==The complex structure of pOPH S172C with ligand, ACA== | ||
<StructureSection load='3wl7' size='340' side='right' caption='[[3wl7]], [[Resolution|resolution]] 1.67Å' scene=''> | <StructureSection load='3wl7' size='340' side='right'caption='[[3wl7]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wl7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3wl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_georgiopolitanum Achromobacter georgiopolitanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WL7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=P2D:PENTANE-2,4-DIONE'>P2D</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=P2D:PENTANE-2,4-DIONE'>P2D</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wl5|3wl5]], [[3wl6|3wl6]], [[3wl8|3wl8]], [[3wla|3wla]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wl5|3wl5]], [[3wl6|3wl6]], [[3wl8|3wl8]], [[3wla|3wla]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pvaB ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pvaB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Achromobacter georgiopolitanum])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-diketone_hydrolase Beta-diketone hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.7 3.7.1.7] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wl7 OCA], [https://pdbe.org/3wl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wl7 RCSB], [https://www.ebi.ac.uk/pdbsum/3wl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wl7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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[[Category: Achromobacter georgiopolitanum]] | [[Category: Achromobacter georgiopolitanum]] | ||
[[Category: Beta-diketone hydrolase]] | [[Category: Beta-diketone hydrolase]] | ||
[[Category: Large Structures]] | |||
[[Category: Chan, H C]] | [[Category: Chan, H C]] | ||
[[Category: Chen, J]] | [[Category: Chen, J]] | ||
Revision as of 08:40, 3 August 2022
The complex structure of pOPH S172C with ligand, ACAThe complex structure of pOPH S172C with ligand, ACA
Structural highlights
Publication Abstract from PubMedThe ever-increasing production and use of polyvinyl alcohol (PVA) threaten our environment. Yet PVA can be assimilated by microbes in two steps: oxidation and cleavage. Here we report novel alpha/beta-hydrolase structures of oxidized PVA hydrolase (OPH) from two known PVA-degrading organisms, Sphingopyxis sp. 113P3 and Pseudomonas sp. VM15C, including complexes with substrate analogues, acetylacetone and caprylate. The active site is covered by a lid-like beta-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the CC bond of beta-diketone, although it has a catalytic triad similar to that of most alpha/beta-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving beta-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications. Structural insights into enzymatic degradation of oxidized polyvinyl alcohol.,Yang Y, Ko TP, Liu L, Li J, Huang CH, Chan HC, Ren F, Jia D, Wang AH, Guo RT, Chen J, Du G Chembiochem. 2014 Sep 5;15(13):1882-6. doi: 10.1002/cbic.201402166. Epub 2014 Jul, 8. PMID:25044912[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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