View source for 5nxl


==Formylglycine generating enzyme from T. curvata in complex with Ag(I)==
<StructureSection load='5nxl' size='340' side='right'caption='[[5nxl]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nxl]] 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=5NXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NXL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</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=AG:SILVER+ION'>AG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=5nxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nxl OCA], [https://pdbe.org/5nxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nxl RCSB], [https://www.ebi.ac.uk/pdbsum/5nxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nxl ProSAT]</span></td></tr>
</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;">
== 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<ref>PMID:28544744</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nxl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermomonospora curvata DSM 43183]]
[[Category: Knop M]]
[[Category: Meury M]]
[[Category: Seebeck FP]]