Author: Myllykoski, Matti; Kursula, Petri
Title: Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase Document date: 2017_1_31
ID: 0a3okta0_16
Snippet: The crystal structure of LigT with 2 0 -AMP was superimposed on the corresponding complex of CNPase, in order to distinguish common and divergent ligand binding determinants in 2H enzymes. The binding mode of the reaction product is very similar in both enzymes, and the base and sugar moieties make similar interactions. While in CNPase, the N terminus of helix α7 is important in coordinating the reaction product [17] , Arg130 is an important res.....
Document: The crystal structure of LigT with 2 0 -AMP was superimposed on the corresponding complex of CNPase, in order to distinguish common and divergent ligand binding determinants in 2H enzymes. The binding mode of the reaction product is very similar in both enzymes, and the base and sugar moieties make similar interactions. While in CNPase, the N terminus of helix α7 is important in coordinating the reaction product [17] , Arg130 is an important residue for binding the corresponding phosphate group in LigT ( Fig 3A) .
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