This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7vem
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='7vem' size='340' side='right'caption='[[7vem]], [[Resolution|resolution]] 2.39Å' scene=''> | <StructureSection load='7vem' size='340' side='right'caption='[[7vem]], [[Resolution|resolution]] 2.39Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VEM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 2.39Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=7vem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vem OCA], [https://pdbe.org/7vem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vem RCSB], [https://www.ebi.ac.uk/pdbsum/7vem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vem 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=7vem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vem OCA], [https://pdbe.org/7vem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vem RCSB], [https://www.ebi.ac.uk/pdbsum/7vem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vem ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Soluble quinone oxidoreductases catalyze transfer of electrons from NADPH to quinones. Transfer of electrons is essential for detoxification of synthetic compounds. Here, we present the crystal structure of a NADPH-dependent QOR from Phytophthora capsici (Pc) complexed with NADPH at 2.4 A resolution. The enzyme exhibits a bi-modular architecture, containing a NADPH-binding groove and a substrate-binding pocket in each subunit. In the crystal, each asymmetric unit of PcQOR contains two molecules stabilized by intermolecular interactions. Gel filtration and ultracentrifugation analyses reveal that it functions as a tetramer in solution. Alignment of homologous structures exhibits a conserved topology. However, the active sites vary among the homologues, indicating differences in substrate specificities. Enzymatic assays indicate that PcQOR tends to catalyze the large substrates, like 9,10-phenanthrenequinone. Computational simulation associated with site-directed mutagenesis and enzymatic activity analysis declares a potential quinone-binding channel. The ability to reduce quinones probably helps P. capsici to detoxify some harmful chemicals encountered during invasion. | ||
| - | |||
| - | Structural Insights into the NAD(P)H:Quinone Oxidoreductase from Phytophthora capsici.,Yang C, Huang Z, Zhang X, Zhu C ACS Omega. 2022 Jul 13;7(29):25705-25714. doi: 10.1021/acsomega.2c02954. , eCollection 2022 Jul 26. PMID:35910145<ref>PMID:35910145</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7vem" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Phytophthora capsici LT1534]] | ||
[[Category: Yang CC]] | [[Category: Yang CC]] | ||
[[Category: Zhu CY]] | [[Category: Zhu CY]] | ||
Current revision
the NADPH-assisted quinone oxidoreductase from Phytophthora capsici
| |||||||||||
