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| | <StructureSection load='1f26' size='340' side='right'caption='[[1f26]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='1f26' size='340' side='right'caption='[[1f26]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1f26]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_144134 Cbs 144134]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F26 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1f26]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F26 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</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]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f24|1f24]], [[1f25|1f25]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitric-oxide_reductase_(cytochrome_c) Nitric-oxide reductase (cytochrome c)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.5 1.7.2.5] </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=1f26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f26 OCA], [https://pdbe.org/1f26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f26 RCSB], [https://www.ebi.ac.uk/pdbsum/1f26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f26 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=1f26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f26 OCA], [https://pdbe.org/1f26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f26 RCSB], [https://www.ebi.ac.uk/pdbsum/1f26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f26 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NOR_FUSOX NOR_FUSOX]] Nitric oxide reductase which is involved in a dissimilatory reduction of nitrite. Acts as a nitric oxide reductase. Is able to reduce nitrate and nitrite to a gaseous form of N(2)O when oxygen supply is limited or discontinued. May function as a detoxification mechanism.<ref>PMID:2040619</ref> <ref>PMID:12105197</ref>
| + | [https://www.uniprot.org/uniprot/NOR_FUSOX NOR_FUSOX] Nitric oxide reductase which is involved in a dissimilatory reduction of nitrite. Acts as a nitric oxide reductase. Is able to reduce nitrate and nitrite to a gaseous form of N(2)O when oxygen supply is limited or discontinued. May function as a detoxification mechanism.<ref>PMID:2040619</ref> <ref>PMID:12105197</ref> |
| | == 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: Cbs 144134]] | + | [[Category: Fusarium oxysporum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Park, S Y]] | + | [[Category: Park S-Y]] |
| - | [[Category: Shimizu, H]] | + | [[Category: Shimizu H]] |
| - | [[Category: Cytochrome p450nor]]
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| - | [[Category: Nitric oxide reductase]]
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| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
NOR_FUSOX Nitric oxide reductase which is involved in a dissimilatory reduction of nitrite. Acts as a nitric oxide reductase. Is able to reduce nitrate and nitrite to a gaseous form of N(2)O when oxygen supply is limited or discontinued. May function as a detoxification mechanism.[1] [2]
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
Threonine 243 of cytochrome P450nor (fungal nitric oxide reductase) corresponds to the 'conserved' Thr in the long I helix of monooxygenase cytochrome P450s. In P450nor, the replacement of Thr243 with Asn, Ala or Val makes the enzymatic activity dramatically reduce. In order to understand the roles of Thr243 in the reduction reaction of NO by P450nor, the crystal structures of three Thr243 mutants (Thr243-->Asn, Thr243-->Val, Thr243-->Ala) of P450nor were determined at a 1.4-A resolution and at cryogenic temperature. However, the hydrogen-bonding pattern in the heme pocket of these mutants is essentially similar for that of the WT enzyme. This suggests that the determination of the structure of the NADH complex of P450nor is required, in order to evaluate the role of Thr243 in its enzymatic reaction. We attempted to crystallize the NADH complex under several conditions, but have not yet been successful.
Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function.,Obayashi E, Shimizu H, Park SY, Shoun H, Shiro Y J Inorg Biochem. 2000 Nov;82(1-4):103-11. PMID:11132616[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shoun H, Tanimoto T. Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction. J Biol Chem. 1991 Jun 15;266(17):11078-82. PMID:2040619
- ↑ Zhang L, Kudo T, Takaya N, Shoun H. The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH. J Biol Chem. 2002 Sep 13;277(37):33842-7. Epub 2002 Jul 8. PMID:12105197 doi:http://dx.doi.org/10.1074/jbc.M203923200
- ↑ Obayashi E, Shimizu H, Park SY, Shoun H, Shiro Y. Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function. J Inorg Biochem. 2000 Nov;82(1-4):103-11. PMID:11132616
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