5NYY

Formylglycine generating enzyme from T. curvata in complex with Cd(II)

5NYY の概要

• エントリーDOI: 10.2210/pdb5nyy/pdb
• 分子名称: Non-specific serine/threonine protein kinase, CADMIUM ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (7 entities in total)
• 機能のキーワード: formylglycine generating enzyme, sulfatase modification, metal-binding, cadmium complex, copper enzyme, transferase
• 由来する生物種: Thermomonospora curvata DSM 43183
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33688.58

構造登録者

Meury, M.,Knop, M.,Seebeck, F.P. (登録日: 2017-05-12, 公開日: 2017-06-07, 最終更新日: 2024-01-17)

主引用文献

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

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: 28544744
DOI: 10.1002/anie.201702901

実験手法

X-RAY DIFFRACTION (1.28 Å)