Selected article for: "active site and family enzyme"
Author: Myllykoski, Matti; Kursula, Petri
Title: Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase
  • Document date: 2017_1_31
    • ID: 0a3okta0_35
    Snippet: Despite the current lack of identity of the physiological activity of LigT, the crystal structures presented here further highlight the versatility of the active-site architectures in 2H phosphoesterases. The best-characterized 2H enzyme is mammalian myelin CNPase, for which a central role in the reaction mechanism is played by the N terminus of helix α7 [17] . This helix is missing in most 2H family members, including LigT, and therefore, the r.....
    Document: Despite the current lack of identity of the physiological activity of LigT, the crystal structures presented here further highlight the versatility of the active-site architectures in 2H phosphoesterases. The best-characterized 2H enzyme is mammalian myelin CNPase, for which a central role in the reaction mechanism is played by the N terminus of helix α7 [17] . This helix is missing in most 2H family members, including LigT, and therefore, the reaction mechanisms must also be different across the enzyme family. The α7 helix blocks access of larger nucleophiles than water into the CNPase active site, and it could be argued that its absence in LigT and most other 2H enzymes hints towards larger molecules, most likely RNA, as potential nucleophiles.

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