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| | <StructureSection load='3ef6' size='340' side='right'caption='[[3ef6]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='3ef6' size='340' side='right'caption='[[3ef6]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ef6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Psep1 Psep1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EF6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ef6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_F1 Pseudomonas putida F1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EF6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dqy|3dqy]], [[3en1|3en1]], [[3eqq|3eqq]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pput_2878, todA, todC1C2BA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=351746 PSEP1])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferredoxin--NAD(+)_reductase Ferredoxin--NAD(+) reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.3 1.18.1.3] </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=3ef6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ef6 OCA], [https://pdbe.org/3ef6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ef6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ef6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ef6 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=3ef6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ef6 OCA], [https://pdbe.org/3ef6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ef6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ef6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ef6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TODA_PSEP1 TODA_PSEP1]] Part of the electron transfer component of toluene 1,2-dioxygenase, transfers electrons from ferredoxin (TodB) to NADH.
| + | [https://www.uniprot.org/uniprot/TODA_PSEP1 TODA_PSEP1] Part of the electron transfer component of toluene 1,2-dioxygenase, transfers electrons from ferredoxin (TodB) to NADH. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psep1]] | + | [[Category: Pseudomonas putida F1]] |
| - | [[Category: Brown, E N]] | + | [[Category: Brown EN]] |
| - | [[Category: Eklund, H]] | + | [[Category: Eklund H]] |
| - | [[Category: Friemann, R]] | + | [[Category: Friemann R]] |
| - | [[Category: Gibson, D T]] | + | [[Category: Gibson DT]] |
| - | [[Category: Lee, K]] | + | [[Category: Lee K]] |
| - | [[Category: Ramaswamy, S]] | + | [[Category: Ramaswamy S]] |
| - | [[Category: Aromatic hydrocarbons catabolism]]
| + | |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Fad binding protein]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Nad]]
| + | |
| - | [[Category: Nadh binding protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
TODA_PSEP1 Part of the electron transfer component of toluene 1,2-dioxygenase, transfers electrons from ferredoxin (TodB) to NADH.
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
Bacterial Rieske non-heme iron oxygenases catalyze the initial hydroxylation of aromatic hydrocarbon substrates. The structures of all three components of one such system, the toluene 2,3-dioxygenase system, have now been determined. This system consists of a reductase, a ferredoxin and a terminal dioxygenase. The dioxygenase, which was cocrystallized with toluene, is a heterohexamer containing a catalytic and a structural subunit. The catalytic subunit contains a Rieske [2Fe-2S] cluster and mononuclear iron at the active site. This iron is not strongly bound and is easily removed during enzyme purification. The structures of the enzyme with and without mononuclear iron demonstrate that part of the structure is flexible in the absence of iron. The orientation of the toluene substrate in the active site is consistent with the regiospecificity of oxygen incorporation seen in the product formed. The ferredoxin is Rieske type and contains a [2Fe-2S] cluster close to the protein surface. The reductase belongs to the glutathione reductase family of flavoenzymes and consists of three domains: an FAD-binding domain, an NADH-binding domain and a C-terminal domain. A model for electron transfer from NADH via FAD in the reductase and the ferredoxin to the terminal active-site mononuclear iron of the dioxygenase is proposed.
Structures of the multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system.,Friemann R, Lee K, Brown EN, Gibson DT, Eklund H, Ramaswamy S Acta Crystallogr D Biol Crystallogr. 2009 Jan;65(Pt 1):24-33. Epub 2008, Dec 18. PMID:19153463[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Friemann R, Lee K, Brown EN, Gibson DT, Eklund H, Ramaswamy S. Structures of the multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system. Acta Crystallogr D Biol Crystallogr. 2009 Jan;65(Pt 1):24-33. Epub 2008, Dec 18. PMID:19153463 doi:10.1107/S0907444908036524
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