Author: Myllykoski, Matti; Kursula, Petri
Title: Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase Document date: 2017_1_31
ID: 0a3okta0_22
Snippet: The active site is surrounded by several loops, which might provide flexibility in substrate binding. The α5-β6 loop, which emerges from helix α5 and leads to the strand β6 that contains one half of the catalytic residues, is disordered in many structures, but can be resolved in selected monomers in the different crystal forms. In mouse CNPase, this loop corresponds to the mobile loop α6-β5, which may play a role in CNPase interaction with .....
Document: The active site is surrounded by several loops, which might provide flexibility in substrate binding. The α5-β6 loop, which emerges from helix α5 and leads to the strand β6 that contains one half of the catalytic residues, is disordered in many structures, but can be resolved in selected monomers in the different crystal forms. In mouse CNPase, this loop corresponds to the mobile loop α6-β5, which may play a role in CNPase interaction with larger substrates. Other flexible loops close to the LigT active site include the C-terminal hairpin loop β8-β9 and the loop connecting strands β4 and β5.
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