3wl5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of pOPH S172C== | |
| + | <StructureSection load='3wl5' size='340' side='right'caption='[[3wl5]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3wl5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WL5 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]] 1.6Å</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=OCS:CYSTEINESULFONIC+ACID'>OCS</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=3wl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wl5 OCA], [https://pdbe.org/3wl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wl5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wl5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OPH_PSESP OPH_PSESP] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 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<ref>PMID:25044912</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3wl5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas sp]] | ||
| + | [[Category: Chan HC]] | ||
| + | [[Category: Chen J]] | ||
| + | [[Category: Du GC]] | ||
| + | [[Category: Guo RT]] | ||
| + | [[Category: Huang CH]] | ||
| + | [[Category: Jia DX]] | ||
| + | [[Category: Ko TP]] | ||
| + | [[Category: Li JH]] | ||
| + | [[Category: Liu L]] | ||
| + | [[Category: Ren FF]] | ||
| + | [[Category: Wang AH-J]] | ||
| + | [[Category: Yang Y]] | ||
Current revision
Crystal structure of pOPH S172C
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Categories: Large Structures | Pseudomonas sp | Chan HC | Chen J | Du GC | Guo RT | Huang CH | Jia DX | Ko TP | Li JH | Liu L | Ren FF | Wang AH-J | Yang Y
