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| | ==Crystal structures of Pseudomonas syringae pv. Tomato DC3000 quinone oxidoreductase complexed with NADPH== | | ==Crystal structures of Pseudomonas syringae pv. Tomato DC3000 quinone oxidoreductase complexed with NADPH== |
| - | <StructureSection load='3jyn' size='340' side='right' caption='[[3jyn]], [[Resolution|resolution]] 2.01Å' scene=''> | + | <StructureSection load='3jyn' size='340' side='right'caption='[[3jyn]], [[Resolution|resolution]] 2.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3jyn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_tomato"_(okabe_1933)_alstatt_1944 "pseudomonas tomato" (okabe 1933) alstatt 1944]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JYN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3jyn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JYN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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]] 2.01Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jyl|3jyl]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH:quinone_reductase NADPH:quinone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.5 1.6.5.5] </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=3jyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jyn OCA], [https://pdbe.org/3jyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jyn RCSB], [https://www.ebi.ac.uk/pdbsum/3jyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jyn ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3jyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jyn OCA], [http://pdbe.org/3jyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jyn RCSB], [http://www.ebi.ac.uk/pdbsum/3jyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jyn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q88B47_PSESM Q88B47_PSESM] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: NADPH:quinone reductase]] | + | [[Category: Large Structures]] |
| - | [[Category: Chang, W]] | + | [[Category: Pseudomonas syringae pv. tomato]] |
| - | [[Category: Gao, Y]] | + | [[Category: Chang W]] |
| - | [[Category: Li, M]] | + | [[Category: Gao Y]] |
| - | [[Category: Pan, X]] | + | [[Category: Li M]] |
| - | [[Category: Zhang, H]] | + | [[Category: Pan X]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Zhang H]] |
| - | [[Category: Protein-nadph complex]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
Q88B47_PSESM
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Zeta-crystallin-like quinone oxidoreductase is NAD(P)H-dependent and catalyzes one-electron reduction of certain quinones to generate semiquinone. Here we present the crystal structures of zeta-crystallin-like quinone oxidoreductase from Pseudomonas syringae pv. tomato DC3000 (PtoQOR) and its complexes with NADPH determined at 2.4 and 2.01A resolutions, respectively. PtoQOR forms as a homologous dimer, each monomer containing two domains. In the structure of the PtoQOR-NADPH complex, NADPH locates in the groove between the two domains. NADPH binding causes obvious conformational changes in the structure of PtoQOR. The putative substrate-binding site of PtoQOR is wider than that of Escherichia coli and Thermus thermophilus HB8. Activity assays show that PtoQOR has weak 1,4-benzoquinone catalytic activity, and very strong reduction activity towards large substrates such as 9,10-phenanthrenequinone. We propose a model to explain the conformational changes which take place during reduction reactions catalyzed by PtoQOR.
Crystal structures of Pseudomonas syringae pv. tomato DC3000 quinone oxidoreductase and its complex with NADPH.,Pan X, Zhang H, Gao Y, Li M, Chang W Biochem Biophys Res Commun. 2009 Dec 18;390(3):597-602. Epub 2009 Oct 8. PMID:19818736[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pan X, Zhang H, Gao Y, Li M, Chang W. Crystal structures of Pseudomonas syringae pv. tomato DC3000 quinone oxidoreductase and its complex with NADPH. Biochem Biophys Res Commun. 2009 Dec 18;390(3):597-602. Epub 2009 Oct 8. PMID:19818736 doi:10.1016/j.bbrc.2009.10.012
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