5NXL
Formylglycine generating enzyme from T. curvata in complex with Ag(I)
Summary for 5NXL
| Entry DOI | 10.2210/pdb5nxl/pdb |
| Descriptor | Non-specific serine/threonine protein kinase, SILVER ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (6 entities in total) |
| Functional Keywords | formylglycine generating enzyme, sulfatase modification, metal-binding, silver complex, copper enzyme, transferase |
| Biological source | Thermomonospora curvata DSM 43183 |
| Total number of polymer chains | 1 |
| Total formula weight | 34097.18 |
| Authors | Meury, M.,Knop, M.,Seebeck, F.P. (deposition date: 2017-05-10, release date: 2017-06-07, Last modification date: 2024-01-17) |
| Primary citation | Meury, M.,Knop, M.,Seebeck, F.P. Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme. Angew. Chem. Int. Ed. Engl., 56:8115-8119, 2017 Cited by PubMed Abstract: The formylglycine-generating enzyme (FGE) is a unique copper protein that catalyzes oxygen-dependent C-H activation. We describe 1.66 Å- and 1.28 Å-resolution crystal structures of FGE from Thermomonospora curvata in complex with either Ag or Cd 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 Cu 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. PubMed: 28544744DOI: 10.1002/anie.201702901 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.66 Å) |
Structure validation
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