View source for 3wla


==Crystal Structure of sOPH Native==
<StructureSection load='3wla' size='340' side='right'caption='[[3wla]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wla]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingopyxis_sp._113P3 Sphingopyxis sp. 113P3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WLA 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3wla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wla OCA], [https://pdbe.org/3wla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wla RCSB], [https://www.ebi.ac.uk/pdbsum/3wla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wla ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OPH_SPHS1 OPH_SPHS1] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wla" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sphingopyxis sp. 113P3]]
[[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]]