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| | <StructureSection load='6e2a' size='340' side='right'caption='[[6e2a]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='6e2a' size='340' side='right'caption='[[6e2a]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <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> | + | <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> |
| - | <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> | + | |
| | <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 == |
| - | [[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>
| + | [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]] |
| - | [[Category: Nitronate monooxygenase]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Pseae]]
| + | [[Category: Agniswamy J]] |
| - | [[Category: Agniswamy, J]] | + | [[Category: Ball J]] |
| - | [[Category: Ball, J]] | + | [[Category: Gadda G]] |
| - | [[Category: Gadda, G]] | + | [[Category: Reis RAG]] |
| - | [[Category: Reis, R A.G]] | + | [[Category: Weber I]] |
| - | [[Category: Weber, I]] | + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Nad+ complex]]
| + | |
| - | [[Category: Nadh:quinone reductase]]
| + | |
| - | [[Category: Oxidative stress]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Quinone]]
| + | |
| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
The crystal structure of the NADH:quinone oxidoreductase PA1024 has been solved in complex with NAD(+) to 2.2 A resolution. The nicotinamide C4 is 3.6 A from the FMN N5 atom, with a suitable orientation for facile hydride transfer. NAD(+) binds in a folded conformation at the interface of the TIM-barrel domain and the extended domain of the enzyme. Comparison of the enzyme-NAD(+) structure with that of the ligand-free enzyme revealed a different conformation of a short loop (75-86) that is part of the NAD(+) -binding pocket. P78, P82, and P84 provide internal rigidity to the loop, whereas Q80 serves as an active site latch that secures the NAD(+) within the binding pocket. An interrupted helix consisting of two alpha-helices connected by a small three-residue loop binds the pyrophosphate moiety of NAD(+) . The adenine moiety of NAD(+) appears to pi-pi stack with Y261. Steric constraints between the adenosine ribose of NAD(+) , P78, and Q80, control the strict specificity of the enzyme for NADH. Charged residues do not play a role in the specificity of PA1024 for the NADH substrate.
Steric hindrance controls pyridine nucleotide specificity of a flavin-dependent NADH:quinone oxidoreductase.,Ball J, Reis RAG, Agniswamy J, Weber IT, Gadda G Protein Sci. 2019 Jan;28(1):167-175. doi: 10.1002/pro.3514. Epub 2018 Oct 31. PMID:30246917[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ball J, Salvi F, Gadda G. Functional Annotation of a Presumed Nitronate Monoxygenase Reveals a New Class of NADH:Quinone Reductases. J Biol Chem. 2016 Sep 30;291(40):21160-21170. PMID:27502282 doi:10.1074/jbc.M116.739151
- ↑ Ball J, Reis RAG, Agniswamy J, Weber IT, Gadda G. Steric hindrance controls pyridine nucleotide specificity of a flavin-dependent NADH:quinone oxidoreductase. Protein Sci. 2019 Jan;28(1):167-175. doi: 10.1002/pro.3514. Epub 2018 Oct 31. PMID:30246917 doi:http://dx.doi.org/10.1002/pro.3514
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