6s07
From Proteopedia
(Difference between revisions)
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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. 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 [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> |
</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='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> | ||
<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='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='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='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='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> | <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> | ||
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== 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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:31588272</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6s07" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Formylglycine-generating enzyme]] | [[Category: Formylglycine-generating enzyme]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Thecd]] | ||
[[Category: Leisinger, F]] | [[Category: Leisinger, F]] | ||
[[Category: Miarzlou, D A]] | [[Category: Miarzlou, D A]] | ||
Revision as of 07:43, 16 October 2019
Structure of formylglycine-generating enzyme at 1.04 A in complex with copper and substrate reveals an acidic pocket for binding and acti-vation of molecular oxygen.
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