Author: Myllykoski, Matti; Kursula, Petri
Title: Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase Document date: 2017_1_31
ID: 0a3okta0_18
Snippet: Within the active site region, the presence of helix α7 in CNPase is a major difference (Fig 4A) . The CNPase-specific helix α7 is missing in LigT, as predicted based on sequence analysis and a structure-based alignment (Fig 4B) . CNPase is the only known 2H phosphoesterase family protein with helix α7 and also the only one, for which the catalytic mechanism has been structurally characterized in detail [5, [15] [16] [17] 19 ]......
Document: Within the active site region, the presence of helix α7 in CNPase is a major difference (Fig 4A) . The CNPase-specific helix α7 is missing in LigT, as predicted based on sequence analysis and a structure-based alignment (Fig 4B) . CNPase is the only known 2H phosphoesterase family protein with helix α7 and also the only one, for which the catalytic mechanism has been structurally characterized in detail [5, [15] [16] [17] 19 ].
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