Structural highlights
5nyy is a 1 chain structure with sequence from Thecd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| Gene: | Tcur_4811 (THECD) |
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
