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| | ==Structure of protoporphyrinogen oxidase from Myxococcus xanthus with acifluorfen== | | ==Structure of protoporphyrinogen oxidase from Myxococcus xanthus with acifluorfen== |
| - | <StructureSection load='2ivd' size='340' side='right' caption='[[2ivd]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2ivd' size='340' side='right'caption='[[2ivd]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ivd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IVD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ivd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IVD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACJ:5-[2-CHLORO-4-(TRIFLUOROMETHYL)PHENOXY]-2-NITROBENZOIC+ACID'>ACJ</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TWN:(3S)-3-[(2S,3S,4R)-3,4-DIMETHYLTETRAHYDROFURAN-2-YL]BUTYL+LAURATE'>TWN</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ive|2ive]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACJ:5-[2-CHLORO-4-(TRIFLUOROMETHYL)PHENOXY]-2-NITROBENZOIC+ACID'>ACJ</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TWN:(3S)-3-[(2S,3S,4R)-3,4-DIMETHYLTETRAHYDROFURAN-2-YL]BUTYL+LAURATE'>TWN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protoporphyrinogen_oxidase Protoporphyrinogen oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.4 1.3.3.4] </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=2ivd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ivd OCA], [https://pdbe.org/2ivd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ivd RCSB], [https://www.ebi.ac.uk/pdbsum/2ivd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ivd 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=2ivd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ivd OCA], [http://pdbe.org/2ivd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ivd RCSB], [http://www.ebi.ac.uk/pdbsum/2ivd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ivd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PGOX_MYXXA PGOX_MYXXA] Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX (PubMed:8621504). Does not oxidize coproporphyrinogen III (PubMed:8621504). Involved in the classical protoporphyrin-dependent (PPD) heme b biosynthesis (PubMed:28123057).<ref>PMID:8621504</ref> <ref>PMID:28123057</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: Atcc 25232]] | + | [[Category: Large Structures]] |
| - | [[Category: Protoporphyrinogen oxidase]] | + | [[Category: Myxococcus xanthus]] |
| - | [[Category: Acharya, K R]] | + | [[Category: Acharya KR]] |
| - | [[Category: Boix, E]] | + | [[Category: Boix E]] |
| - | [[Category: Corradi, H R]] | + | [[Category: Corradi HR]] |
| - | [[Category: Corrigall, A V]] | + | [[Category: Corrigall AV]] |
| - | [[Category: Meissner, P N]] | + | [[Category: Meissner PN]] |
| - | [[Category: Mohan, C G]] | + | [[Category: Mohan CG]] |
| - | [[Category: Sturrock, E D]] | + | [[Category: Sturrock ED]] |
| - | [[Category: Acifluorfen]]
| + | |
| - | [[Category: Chlorophyll biosynthesis]]
| + | |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Haem biosynthesis]]
| + | |
| - | [[Category: Heme biosynthesis]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Porphyria]]
| + | |
| - | [[Category: Porphyrin biosynthesis]]
| + | |
| Structural highlights
Function
PGOX_MYXXA Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX (PubMed:8621504). Does not oxidize coproporphyrinogen III (PubMed:8621504). Involved in the classical protoporphyrin-dependent (PPD) heme b biosynthesis (PubMed:28123057).[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
Protoporphyrinogen IX oxidase, a monotopic membrane protein, which catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX in the heme/chlorophyll biosynthetic pathway, is distributed widely throughout nature. Here we present the structure of protoporphyrinogen IX oxidase from Myxococcus xanthus, an enzyme with similar catalytic properties to human protoporphyrinogen IX oxidase that also binds the common plant herbicide, acifluorfen. In the native structure, the planar porphyrinogen substrate is mimicked by a Tween 20 molecule, tracing three sides of the macrocycle. In contrast, acifluorfen does not mimic the planarity of the substrate but is accommodated by the shape of the binding pocket and held in place by electrostatic and aromatic interactions. A hydrophobic patch surrounded by positively charged residues suggests the position of the membrane anchor, differing from the one proposed for the tobacco mitochondrial protoporphyrinogen oxidase. Interestingly, there is a discrepancy between the dimerization state of the protein in solution and in the crystal. Conserved structural features are discussed in relation to a number of South African variegate porphyria-causing mutations in the human enzyme.
Crystal structure of protoporphyrinogen oxidase from Myxococcus xanthus and its complex with the inhibitor acifluorfen.,Corradi HR, Corrigall AV, Boix E, Mohan CG, Sturrock ED, Meissner PN, Acharya KR J Biol Chem. 2006 Dec 15;281(50):38625-33. Epub 2006 Oct 17. PMID:17046834[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dailey HA, Dailey TA. Protoporphyrinogen oxidase of Myxococcus xanthus. Expression, purification, and characterization of the cloned enzyme. J Biol Chem. 1996 Apr 12;271(15):8714-8. PMID:8621504 doi:10.1074/jbc.271.15.8714
- ↑ Dailey HA, Dailey TA, Gerdes S, Jahn D, Jahn M, O'Brian MR, Warren MJ. Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product. Microbiol Mol Biol Rev. 2017 Jan 25;81(1):e00048-16. PMID:28123057 doi:10.1128/MMBR.00048-16
- ↑ Corradi HR, Corrigall AV, Boix E, Mohan CG, Sturrock ED, Meissner PN, Acharya KR. Crystal structure of protoporphyrinogen oxidase from Myxococcus xanthus and its complex with the inhibitor acifluorfen. J Biol Chem. 2006 Dec 15;281(50):38625-33. Epub 2006 Oct 17. PMID:17046834 doi:http://dx.doi.org/10.1074/jbc.M606640200
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