5nxl

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'''Unreleased structure'''
 
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The entry 5nxl is ON HOLD
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==Formylglycine generating enzyme from T. curvata in complex with Ag(I)==
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<StructureSection load='5nxl' size='340' side='right' caption='[[5nxl]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5nxl]] 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=5NXL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NXL FirstGlance]. <br>
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</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=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>
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<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>
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<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>
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<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=5nxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nxl OCA], [http://pdbe.org/5nxl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nxl RCSB], [http://www.ebi.ac.uk/pdbsum/5nxl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nxl ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5nxl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Thecd]]
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[[Category: Knop, M]]
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[[Category: Meury, M]]
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[[Category: Seebeck, F P]]
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[[Category: Copper enzyme]]
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[[Category: Formylglycine generating enzyme]]
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[[Category: Metal-binding]]
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[[Category: Silver complex]]
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[[Category: Sulfatase modification]]
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[[Category: Transferase]]

Revision as of 08:13, 16 November 2017

Formylglycine generating enzyme from T. curvata in complex with Ag(I)

5nxl, resolution 1.66Å

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