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| | <StructureSection load='6s07' size='340' side='right'caption='[[6s07]], [[Resolution|resolution]] 1.04Å' scene=''> | | <StructureSection load='6s07' size='340' side='right'caption='[[6s07]], [[Resolution|resolution]] 1.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6s07]] is a 2 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=6S07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S07 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6s07]] is a 2 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=6S07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S07 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</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]] 1.04Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6s07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s07 OCA], [https://pdbe.org/6s07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s07 RCSB], [https://www.ebi.ac.uk/pdbsum/6s07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s07 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formylglycine-generating_enzyme Formylglycine-generating enzyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.7 1.8.3.7] </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=6s07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s07 OCA], [http://pdbe.org/6s07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s07 RCSB], [http://www.ebi.ac.uk/pdbsum/6s07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s07 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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: Formylglycine-generating enzyme]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thecd]] | + | [[Category: Thermomonospora curvata DSM 43183]] |
| - | [[Category: Leisinger, F]] | + | [[Category: Leisinger F]] |
| - | [[Category: Miarzlou, D A]] | + | [[Category: Miarzlou DA]] |
| - | [[Category: Seebeck, F P]] | + | [[Category: Seebeck FP]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Copper]]
| + | |
| - | [[Category: Substrate analog]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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) catalyzes oxidative conversion of specific peptidyl-cysteine residues to formylglycine. FGE mediates O2-activation and hydrogen-atom abstraction in an active site that contains Cu(i) coordinated to two cysteine residues. Similar coordination geometries are common among copper-sensing transcription factors and copper-chaperone but are unprecedented among copper-dependent oxidases. To examine the mechanism of this unusual catalyst we determined the 1.04 A structure of FGE from Thermomonospora curvata in complex with copper and a cysteine-containing peptide substrate. This structure unveils a network of four crystallographic waters and two active site residues that form a highly acidic O2-binding pocket juxtaposed to the trigonal planar tris-cysteine coordinated Cu(i) center. Comparison with structures of FGE in complex with Ag(i) and Cd(ii) combined with evidence from NMR spectroscopy and kinetic observations highlight several structural changes that are induced by substrate binding and prime the enzyme for O2-binding and subsequent activation.
Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen.,Miarzlou DA, Leisinger F, Joss D, Haussinger D, Seebeck FP Chem Sci. 2019 Jun 18;10(29):7049-7058. doi: 10.1039/c9sc01723b. eCollection 2019, Aug 7. PMID:31588272[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
- ↑ Miarzlou DA, Leisinger F, Joss D, Haussinger D, Seebeck FP. Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen. Chem Sci. 2019 Jun 18;10(29):7049-7058. doi: 10.1039/c9sc01723b. eCollection 2019, Aug 7. PMID:31588272 doi:http://dx.doi.org/10.1039/c9sc01723b
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