View source for 7xwm


==structure of patulin-detoxifying enzyme Y155F/V187K with NADPH==
<StructureSection load='7xwm' size='340' side='right'caption='[[7xwm]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xwm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Meyerozyma_guilliermondii Meyerozyma guilliermondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XWM 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]] 1.98&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=7xwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xwm OCA], [https://pdbe.org/7xwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xwm RCSB], [https://www.ebi.ac.uk/pdbsum/7xwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xwm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A888VSF1_PICGM A0A888VSF1_PICGM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Patulin is a fatal mycotoxin that is widely detected in drinking water and fruit-derived products contaminated by diverse filamentous fungi. CgSDR from Candida guilliermondii represents the first NADPH-dependent short-chain dehydrogenase/reductase that catalyzes the reduction of patulin to the nontoxic E-ascladiol. To elucidate the catalytic mechanism of CgSDR, we solved its crystal structure in complex with cofactor and substrate. Structural analyses indicate that patulin is situated in a hydrophobic pocket adjacent to the cofactor, with the hemiacetal ring orienting toward the nicotinamide moiety of NADPH. In addition, we conducted structure-guided engineering to modify substrate-binding residue V187 and obtained variant V187F, V187K and V187W, whose catalytic activity was elevated by 3.9-, 2.2- and 1.7-fold, respectively. The crystal structures of CgSDR variants suggest that introducing additional aromatic stacking or hydrogen-bonding interactions to bind the lactone ring of patulin might account for the observed enhanced activity. These results illustrate the catalytic mechanism of SDR-mediated patulin detoxification for the first time and provide the upgraded variants that exhibit tremendous potentials in industrial applications.

Structure-based rational design of a short-chain dehydrogenase/reductase for improving activity toward mycotoxin patulin.,Dai L, Li H, Huang JW, Hu Y, He M, Yang Y, Min J, Guo RT, Chen CC Int J Biol Macromol. 2022 Dec 1;222(Pt A):421-428. doi: , 10.1016/j.ijbiomac.2022.09.121. Epub 2022 Sep 20. PMID:36176222<ref>PMID:36176222</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7xwm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Meyerozyma guilliermondii]]
[[Category: Chen CC]]
[[Category: Dai L]]
[[Category: Guo RT]]
[[Category: Hu Y]]
[[Category: Li H]]