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6e2a

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Current revision (06:17, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6e2a' size='340' side='right'caption='[[6e2a]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6e2a' size='340' side='right'caption='[[6e2a]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e2a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E2A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e2a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E2A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA1024 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitronate_monooxygenase Nitronate monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.16 1.13.12.16] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2a OCA], [https://pdbe.org/6e2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e2a RCSB], [https://www.ebi.ac.uk/pdbsum/6e2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2a 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=6e2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2a OCA], [https://pdbe.org/6e2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e2a RCSB], [https://www.ebi.ac.uk/pdbsum/6e2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/2NPD_PSEAE 2NPD_PSEAE]] Catalyzes the oxidative denitrification of nitronates to their corresponding aldehydes and nitrites.<ref>PMID:16682407</ref>
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[https://www.uniprot.org/uniprot/NQRED_PSEAE NQRED_PSEAE] Catalyzes the NADH-dependent reduction of a broad spectrum of quinone substrates, generating the corresponding hydroquinones. Highly prefers NADH to NADPH as a reducing substrate. Also displays a small NADH oxidase activity. Does not exhibit nitronate monooxygenase activity; is inactive against propionate 3-nitronate, 3-nitropropionate, nitroethane, 1-nitropropane, 2-nitropropane, and the anionic forms ethylnitronate, propyl-1-nitronate, and propyl-2-nitronate. Has no azoreductase activity since it is not able to reduce the azo dye methyl red with NADH. May be required to maintain an appropriate [NAD(+)]/[NADH] ratio for the catabolism of fatty acids in P.aeruginosa PAO1.<ref>PMID:27502282</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nitronate monooxygenase]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Pseae]]
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[[Category: Agniswamy J]]
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[[Category: Agniswamy, J]]
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[[Category: Ball J]]
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[[Category: Ball, J]]
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[[Category: Gadda G]]
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[[Category: Gadda, G]]
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[[Category: Reis RAG]]
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[[Category: Reis, R A.G]]
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[[Category: Weber I]]
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[[Category: Weber, I]]
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[[Category: Flavoprotein]]
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[[Category: Nad+ complex]]
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[[Category: Nadh:quinone reductase]]
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[[Category: Oxidative stress]]
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[[Category: Oxidoreductase]]
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[[Category: Quinone]]
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Current revision

Crystal structure of NADH:quinone reductase PA1024 from Pseudomonas aeruginosa PAO1 in complex with NAD+

PDB ID 6e2a

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