Author: Myllykoski, Matti; Kursula, Petri
Title: Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase Document date: 2017_1_31
ID: 0a3okta0_29
Snippet: LigT has been characterized as an enzyme that can ligate tRNA fragments cleaved by yeast endonuclease. The ligation joins the 2 0 ,3 0 -cyclic phosphate and 5 0 -hydroxyl termini in a 2 0 -5 0 phosphodiester linkage, where the linking phosphate group is derived from the cyclic phosphate moiety [10] . Therefore, LigT should bind RNA in the close vicinity of its active site. We looked at the surface properties of LigT to better understand this proc.....
Document: LigT has been characterized as an enzyme that can ligate tRNA fragments cleaved by yeast endonuclease. The ligation joins the 2 0 ,3 0 -cyclic phosphate and 5 0 -hydroxyl termini in a 2 0 -5 0 phosphodiester linkage, where the linking phosphate group is derived from the cyclic phosphate moiety [10] . Therefore, LigT should bind RNA in the close vicinity of its active site. We looked at the surface properties of LigT to better understand this process.
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