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| | ==Formylglycine generating enzyme from T. curvata in complex with Cd(II)== | | ==Formylglycine generating enzyme from T. curvata in complex with Cd(II)== |
| - | <StructureSection load='5nyy' size='340' side='right' caption='[[5nyy]], [[Resolution|resolution]] 1.28Å' scene=''> | + | <StructureSection load='5nyy' size='340' side='right'caption='[[5nyy]], [[Resolution|resolution]] 1.28Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nyy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thecd Thecd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NYY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NYY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nyy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomonospora_curvata_DSM_43183 Thermomonospora curvata DSM 43183]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NYY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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]] 1.28Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tcur_4811 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=471852 THECD])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5nyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nyy OCA], [https://pdbe.org/5nyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nyy RCSB], [https://www.ebi.ac.uk/pdbsum/5nyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nyy 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=5nyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nyy OCA], [http://pdbe.org/5nyy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nyy RCSB], [http://www.ebi.ac.uk/pdbsum/5nyy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nyy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FGE_THECD FGE_THECD] Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile.<ref>PMID:26403223</ref> <ref>PMID:27862795</ref> |
| | <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: Non-specific serine/threonine protein kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Thecd]] | + | [[Category: Thermomonospora curvata DSM 43183]] |
| - | [[Category: Knop, M]] | + | [[Category: Knop M]] |
| - | [[Category: Meury, M]] | + | [[Category: Meury M]] |
| - | [[Category: Seebeck, F P]] | + | [[Category: Seebeck FP]] |
| - | [[Category: Cadmium complex]]
| + | |
| - | [[Category: Copper enzyme]]
| + | |
| - | [[Category: Formylglycine generating enzyme]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Sulfatase modification]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
5nyy is a 1 chain structure with sequence from Thermomonospora curvata DSM 43183. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.28Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
FGE_THECD Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile.[1] [2]
Publication Abstract from PubMed
The formylglycine-generating enzyme (FGE) is a unique copper protein that catalyzes oxygen-dependent C-H activation. We describe 1.66 A- and 1.28 A-resolution crystal structures of FGE from Thermomonospora curvata in complex with either AgI or CdII providing definitive evidence for a high-affinity metal-binding site in this enzyme. The structures reveal a bis-cysteine linear coordination of the monovalent metal, and tetrahedral coordination of the bivalent metal. Similar coordination changes may occur in the active enzyme as a result of CuI/II redox cycling. Complexation of copper atoms by two cysteine residues is common among copper-trafficking proteins, but is unprecedented for redox-active copper enzymes or synthetic copper catalysts.
Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme.,Meury M, Knop M, Seebeck FP Angew Chem Int Ed Engl. 2017 Jul 3;56(28):8115-8119. doi: 10.1002/anie.201702901., Epub 2017 Jun 9. PMID:28544744[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Knop M, Engi P, Lemnaru R, Seebeck FP. In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I). Chembiochem. 2015 Oct 12;16(15):2147-50. doi: 10.1002/cbic.201500322. Epub 2015, Sep 25. PMID:26403223 doi:http://dx.doi.org/10.1002/cbic.201500322
- ↑ Knop M, Dang TQ, Jeschke G, Seebeck FP. Copper is a Cofactor of the Formylglycine-Generating Enzyme. Chembiochem. 2017 Jan 17;18(2):161-165. doi: 10.1002/cbic.201600359. Epub 2016, Dec 13. PMID:27862795 doi:http://dx.doi.org/10.1002/cbic.201600359
- ↑ Meury M, Knop M, Seebeck FP. Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme. Angew Chem Int Ed Engl. 2017 Jul 3;56(28):8115-8119. doi: 10.1002/anie.201702901., Epub 2017 Jun 9. PMID:28544744 doi:http://dx.doi.org/10.1002/anie.201702901
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