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| | <StructureSection load='4tlf' size='340' side='right'caption='[[4tlf]], [[Resolution|resolution]] 2.14Å' scene=''> | | <StructureSection load='4tlf' size='340' side='right'caption='[[4tlf]], [[Resolution|resolution]] 2.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tlf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TLF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TLF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tlf]] is a 4 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=4TLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TLF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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]] 2.137Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA2602, NC002516.2 ([http://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=FE2:FE+(II)+ION'>FE2</scene></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=4tlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tlf OCA], [http://pdbe.org/4tlf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tlf RCSB], [http://www.ebi.ac.uk/pdbsum/4tlf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tlf 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=4tlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tlf OCA], [https://pdbe.org/4tlf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tlf RCSB], [https://www.ebi.ac.uk/pdbsum/4tlf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tlf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/3MDO_PSEAE 3MDO_PSEAE] Thiol dioxygenase that catalyzes the dioxygenation of 3-mercaptopropionate (3-MPA) to 3-sulfinopropionate (3-SPA). To a lesser extent (40-fold lower efficiency), is also able to oxidize cysteine to cysteine sulfinate (CSA). Cannot use N-acetyl-L-cysteine, homocysteine, and cysteamine as substrates. The physiological role of this enzyme is unclear.<ref>PMID:26272617</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Dioxygenase|Dioxygenase]] | + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: FELLNER, M]] | + | [[Category: Fellner M]] |
| - | [[Category: Jameson, G N.L]] | + | [[Category: Jameson GNL]] |
| - | [[Category: Tchesnokov, E P]] | + | [[Category: Tchesnokov EP]] |
| - | [[Category: Wilbanks, S M]] | + | [[Category: Wilbanks SM]] |
| - | [[Category: 3-mpa dioxygenase]]
| + | |
| - | [[Category: Cupin]]
| + | |
| - | [[Category: Cysteine dioxygenase]]
| + | |
| - | [[Category: Non-heme mono-iron]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Pseudomonas aeruginosa]]
| + | |
| - | [[Category: Thiol dioxygenase]]
| + | |
| Structural highlights
Function
3MDO_PSEAE Thiol dioxygenase that catalyzes the dioxygenation of 3-mercaptopropionate (3-MPA) to 3-sulfinopropionate (3-SPA). To a lesser extent (40-fold lower efficiency), is also able to oxidize cysteine to cysteine sulfinate (CSA). Cannot use N-acetyl-L-cysteine, homocysteine, and cysteamine as substrates. The physiological role of this enzyme is unclear.[1]
Publication Abstract from PubMed
Thiol dioxygenation is the initial oxidation step that commits a thiol to important catabolic or biosynthetic pathways. The reaction is catalyzed by a family of specific non-heme mononuclear-iron proteins each of which is reported to react efficiently with only one substrate. This family of enzymes includes cysteine dioxygenase, cysteamine dioxygenase, mercaptosuccinate dioxygenase and 3-mercaptopropionate dioxygenase. Using sequence alignment to infer cysteine dioxygenase activity, a cysteine dioxygenase homologue from Pseudomonas aeruginosa (p3MDO) has been identified. Mass spectrometry of P. aeruginosa under standard growth conditions showed p3MDO is expressed in low levels suggesting that this metabolic pathway is available to the organism. Purified recombinant p3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid (3-MPA) in vitro, with a marked preference for 3-MPA. We therefore describe this enzyme as a 3-mercaptopropionate dioxygenase. Mossbauer spectroscopy suggests that substrate binding to the ferrous iron is through the thiol but indicates each substrate could adopt different coordination geometries. Crystallographic comparison with mammalian cysteine dioxygenase shows that the overall active site geometry is conserved but suggests that the different substrate specificity can be related to replacement of an arginine by a glutamine in the active site.
The Cysteine Dioxygenase Homologue from Pseudomonas aeruginosa is a 3-Mercaptopropionate Dioxygenase.,Tchesnokov EP, Fellner M, Siakkou E, Kleffmann T, Martin LW, Aloi S, Lamont IL, Wilbanks SM, Jameson GN J Biol Chem. 2015 Aug 13. pii: jbc.M114.635672. PMID:26272617[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tchesnokov EP, Fellner M, Siakkou E, Kleffmann T, Martin LW, Aloi S, Lamont IL, Wilbanks SM, Jameson GN. The Cysteine Dioxygenase Homologue from Pseudomonas aeruginosa is a 3-Mercaptopropionate Dioxygenase. J Biol Chem. 2015 Aug 13. pii: jbc.M114.635672. PMID:26272617 doi:http://dx.doi.org/10.1074/jbc.M114.635672
- ↑ Tchesnokov EP, Fellner M, Siakkou E, Kleffmann T, Martin LW, Aloi S, Lamont IL, Wilbanks SM, Jameson GN. The Cysteine Dioxygenase Homologue from Pseudomonas aeruginosa is a 3-Mercaptopropionate Dioxygenase. J Biol Chem. 2015 Aug 13. pii: jbc.M114.635672. PMID:26272617 doi:http://dx.doi.org/10.1074/jbc.M114.635672
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