Author: Myllykoski, Matti; Kursula, Petri
Title: Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase Document date: 2017_1_31
ID: 0a3okta0_14
Snippet: In addition, attempts to cocrystallize LigT with tRNA resulted in a structure with apparent phosphate ions bound to the active site; these probably originated as impurities in the tRNA preparation. Two distinct PO 4 -binding sites are observed in the active site, on both sides of Arg130 (Fig 2D) . Their locations could correspond to binding sites for phosphomoieties in a bound RNA substrate. One of the phosphates lies in the active site, while th.....
Document: In addition, attempts to cocrystallize LigT with tRNA resulted in a structure with apparent phosphate ions bound to the active site; these probably originated as impurities in the tRNA preparation. Two distinct PO 4 -binding sites are observed in the active site, on both sides of Arg130 (Fig 2D) . Their locations could correspond to binding sites for phosphomoieties in a bound RNA substrate. One of the phosphates lies in the active site, while the second is in a nearby cavity, close to Arg35. The density for the second phosphate molecule was strongest in monomer D, and it was not built into the other three monomers in the model, as the electron density suggested only partial occupancy.
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