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| | <StructureSection load='3d9g' size='340' side='right'caption='[[3d9g]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='3d9g' size='340' side='right'caption='[[3d9g]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3d9g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Fusox Fusox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D9G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3d9g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusox Fusox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D9G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CNX:HEPTANENITRILE'>CNX</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CNX:HEPTANENITRILE'>CNX</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c12|2c12]], [[2c0u|2c0u]], [[2reh|2reh]], [[2zaf|2zaf]], [[3d9d|3d9d]], [[3d9e|3d9e]], [[3d9f|3d9f]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c12|2c12]], [[2c0u|2c0u]], [[2reh|2reh]], [[2zaf|2zaf]], [[3d9d|3d9d]], [[3d9e|3d9e]], [[3d9f|3d9f]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitroalkane_oxidase Nitroalkane oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.1 1.7.3.1] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitroalkane_oxidase Nitroalkane oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.1 1.7.3.1] </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=3d9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d9g OCA], [http://pdbe.org/3d9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d9g RCSB], [http://www.ebi.ac.uk/pdbsum/3d9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d9g 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=3d9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d9g OCA], [https://pdbe.org/3d9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d9g RCSB], [https://www.ebi.ac.uk/pdbsum/3d9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d9g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NAO_FUSOX NAO_FUSOX]] Catalyzes the oxidative denitrification of neutral nitroalkanes, including 3-nitro-2-pentanol, 1-nitropropane, 2-nitropropane, nitroethane and nitrocyclohexane, and may thereby protect the organism against toxic compounds. Has no detectable acyl-CoA dehydrogenase activity.<ref>PMID:11867731</ref> <ref>PMID:22538</ref> <ref>PMID:16430210</ref> | + | [[https://www.uniprot.org/uniprot/NAO_FUSOX NAO_FUSOX]] Catalyzes the oxidative denitrification of neutral nitroalkanes, including 3-nitro-2-pentanol, 1-nitropropane, 2-nitropropane, nitroethane and nitrocyclohexane, and may thereby protect the organism against toxic compounds. Has no detectable acyl-CoA dehydrogenase activity.<ref>PMID:11867731</ref> <ref>PMID:22538</ref> <ref>PMID:16430210</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[NAO_FUSOX] Catalyzes the oxidative denitrification of neutral nitroalkanes, including 3-nitro-2-pentanol, 1-nitropropane, 2-nitropropane, nitroethane and nitrocyclohexane, and may thereby protect the organism against toxic compounds. Has no detectable acyl-CoA dehydrogenase activity.[1] [2] [3]
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
The flavoenzyme nitroalkane oxidase is a member of the acyl-CoA dehydrogenase superfamily. Nitroalkane oxidase catalyzes the oxidation of neutral nitroalkanes to nitrite and the corresponding aldehydes or ketones. Crystal structures to 2.2 A resolution or better of enzyme complexes with bound substrates and of a trapped substrate-flavin adduct are described. The D402N enzyme has no detectable activity with neutral nitroalkanes [Valley, M. P., and Fitzpatrick, P. F. (2003) J. Am. Chem. Soc. 125, 8738-8739]. The structure of the D402N enzyme crystallized in the presence of 1-nitrohexane or 1-nitrooctane shows the presence of the substrate in the binding site. The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. The oxygens of the substrate nitro group interact both with amino acid residues and with the 2'-hydroxyl of the FAD. When nitroalkane oxidase oxidizes nitroalkanes in the presence of cyanide, an electrophilic flavin imine intermediate can be trapped [Valley, M. P., Tichy, S. E., and Fitzpatrick, P. F. (2005) J. Am. Chem. Soc. 127, 2062-2066]. The structure of the enzyme trapped with cyanide during oxidation of 1-nitrohexane shows the presence of the modified flavin. A continuous hydrogen bond network connects the nitrogen of the CN-hexyl-FAD through the FAD 2'-hydroxyl to a chain of water molecules extending to the protein surface. Together, our complementary approaches provide strong evidence that the flavin cofactor is in the appropriate oxidation state and correlates well with the putative intermediate state observed within each of the crystal structures. Consequently, these results provide important structural descriptions of several steps along the nitroalkane oxidase reaction cycle.
Crystal Structures of Intermediates in the Nitroalkane Oxidase Reaction (dagger) (double dagger).,Heroux A, Bozinovski DM, Valley MP, Fitzpatrick PF, Orville AM Biochemistry. 2009 Mar 27. PMID:19265437[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Daubner SC, Gadda G, Valley MP, Fitzpatrick PF. Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2702-7. Epub 2002 Feb 26. PMID:11867731 doi:http://dx.doi.org/10.1073/pnas.052527799
- ↑ Kido T, Hashizume K, Soda K. Purification and properties of nitroalkane oxidase from Fusarium oxysporum. J Bacteriol. 1978 Jan;133(1):53-8. PMID:22538
- ↑ Nagpal A, Valley MP, Fitzpatrick PF, Orville AM. Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover. Biochemistry. 2006 Jan 31;45(4):1138-50. PMID:16430210 doi:10.1021/bi051966w
- ↑ Heroux A, Bozinovski DM, Valley MP, Fitzpatrick PF, Orville AM. Crystal Structures of Intermediates in the Nitroalkane Oxidase Reaction (dagger) (double dagger). Biochemistry. 2009 Mar 27. PMID:19265437 doi:10.1021/bi8023042
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