7utf: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7utf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_leguminosarum Rhizobium leguminosarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UTF FirstGlance]. <br> | <table><tr><td colspan='2'>[[7utf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_leguminosarum Rhizobium leguminosarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UTF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <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=7utf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7utf OCA], [https://pdbe.org/7utf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7utf RCSB], [https://www.ebi.ac.uk/pdbsum/7utf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7utf ProSAT]</span></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=7utf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7utf OCA], [https://pdbe.org/7utf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7utf RCSB], [https://www.ebi.ac.uk/pdbsum/7utf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7utf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/J0WHR2_RHILT J0WHR2_RHILT] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 20:20, 18 October 2023
Structure-Function characterization of an aldo-keto reductase involved in detoxification of the mycotoxin, deoxynivalenolStructure-Function characterization of an aldo-keto reductase involved in detoxification of the mycotoxin, deoxynivalenol
Structural highlights
FunctionPublication Abstract from PubMedDeoxynivalenol (DON) is a mycotoxin, produced by filamentous fungi such as Fusarium graminearum, that causes significant yield losses of cereal grain crops worldwide. One of the most promising methods to detoxify this mycotoxin involves its enzymatic epimerization to 3-epi-DON. DepB plays a critical role in this process by reducing 3-keto-DON, an intermediate in the epimerization process, to 3-epi-DON. DepBRleg from Rhizobium leguminosarum is a member of the new aldo-keto reductase family, AKR18, and it has the unusual ability to utilize both NADH and NADPH as coenzymes, albeit with a 40-fold higher catalytic efficiency with NADPH compared to NADH. Structural analysis of DepBRleg revealed the putative roles of Lys-217, Arg-290, and Gln-294 in NADPH specificity. Replacement of these residues by site-specific mutagenesis to negatively charged amino acids compromised NADPH binding with minimal effects on NADH binding. The substrate-binding site of DepBRleg is larger than its closest structural homolog, AKR6A2, likely contributing to its ability to utilize a wide range of aldehydes and ketones, including the mycotoxin, patulin, as substrates. The structure of DepBRleg also suggests that 3-keto-DON can adopt two binding modes to facilitate 4-pro-R hydride transfer to either the re- or si-face of the C3 ketone providing a possible explanation for the enzyme's ability to convert 3-keto-DON to 3-epi-DON and DON in diastereomeric ratios of 67.2% and 32.8% respectively. Structure-function characterization of an aldo-keto reductase involved in detoxification of the mycotoxin, deoxynivalenol.,Abraham N, Schroeter KL, Zhu Y, Chan J, Evans N, Kimber MS, Carere J, Zhou T, Seah SYK Sci Rep. 2022 Aug 30;12(1):14737. doi: 10.1038/s41598-022-19040-8. PMID:36042239[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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