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| | <StructureSection load='6bgm' size='340' side='right'caption='[[6bgm]], [[Resolution|resolution]] 2.21Å' scene=''> | | <StructureSection load='6bgm' size='340' side='right'caption='[[6bgm]], [[Resolution|resolution]] 2.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6bgm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BGM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BGM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bgm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BGM 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>, <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]] 2.206Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_dioxygenase Cysteine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.20 1.13.11.20] </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=6bgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bgm OCA], [https://pdbe.org/6bgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bgm RCSB], [https://www.ebi.ac.uk/pdbsum/6bgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bgm 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=6bgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bgm OCA], [http://pdbe.org/6bgm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bgm RCSB], [http://www.ebi.ac.uk/pdbsum/6bgm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bgm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CDO1_HUMAN CDO1_HUMAN]] Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range. | + | [https://www.uniprot.org/uniprot/CDO1_HUMAN CDO1_HUMAN] Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cysteine dioxygenase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, J]] | + | [[Category: Li J]] |
| - | [[Category: Liu, A]] | + | [[Category: Liu A]] |
| - | [[Category: Shin, I]] | + | [[Category: Shin I]] |
| - | [[Category: Cys-tyr cofactor]]
| + | |
| - | [[Category: Cysteine]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
CDO1_HUMAN Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range.
Publication Abstract from PubMed
Cysteine dioxygenase (CDO) plays an essential role in sulfur metabolism by regulating homeostatic levels of cysteine. Human CDO contains a post-translationally generated Cys93-Tyr157 cross-linked cofactor. Here, we investigated this Cys-Tyr cross-linking by incorporating unnatural tyrosines in place of Tyr157 via a genetic method. The catalytically active variants were obtained with a thioether bond between Cys93 and the halogen-substituted Tyr157, and we determined the crystal structures of both wild-type and engineered CDO variants in the purely uncross-linked form and with a mature cofactor. Along with mass spectrometry and (19)F NMR, these data indicated that the enzyme could catalyze oxidative C-F or C-Cl bond cleavage, resulting in a substantial conformational change of both Cys93 and Tyr157 during cofactor assembly. These findings provide insights into the mechanism of Cys-Tyr cofactor biogenesis and may aid the development of bioinspired aromatic carbon-halogen bond activation.
Cleavage of a carbon-fluorine bond by an engineered cysteine dioxygenase.,Li J, Griffith WP, Davis I, Shin I, Wang J, Li F, Wang Y, Wherritt DJ, Liu A Nat Chem Biol. 2018 Jun 25. pii: 10.1038/s41589-018-0085-5. doi:, 10.1038/s41589-018-0085-5. PMID:29942080[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li J, Griffith WP, Davis I, Shin I, Wang J, Li F, Wang Y, Wherritt DJ, Liu A. Cleavage of a carbon-fluorine bond by an engineered cysteine dioxygenase. Nat Chem Biol. 2018 Jun 25. pii: 10.1038/s41589-018-0085-5. doi:, 10.1038/s41589-018-0085-5. PMID:29942080 doi:http://dx.doi.org/10.1038/s41589-018-0085-5
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