Author: Myllykoski, Matti; Kursula, Petri
Title: Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase Document date: 2017_1_31
ID: 0a3okta0_23
Snippet: The LigT ligand complexes highlight mobility of the LigT loops and possible RNA-interacting residues close to the active site. In different crystal forms, the active-site loops can be observed in slightly different conformations (Fig 5A) , and especially residues Arg6 and Arg35 take different conformations depending on the bound ligand, further implying their role in phosphomoiety recognition. In a ligand-free active site, also Phe48 is seen to t.....
Document: The LigT ligand complexes highlight mobility of the LigT loops and possible RNA-interacting residues close to the active site. In different crystal forms, the active-site loops can be observed in slightly different conformations (Fig 5A) , and especially residues Arg6 and Arg35 take different conformations depending on the bound ligand, further implying their role in phosphomoiety recognition. In a ligand-free active site, also Phe48 is seen to take a conformation distinct from that seen in ligand complexes. Hence, as opposed to CNPase, in which the active site is to a large extent pre-organized for substrate binding [16, 17] , LigT shows more flexibility.
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