id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-002398-0a3okta0	Myllykoski, Matti	Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase	2017-01-31		.txt	text/plain	6151	363	56	Here, we studied the structure of the 2H family member LigT from Escherichia coli both in the apo form and complexed with different active-site ligands, including ATP, 2′-AMP, 3′-AMP, phosphate, and NADP(+). coli LigT bound to tRNA in solution, and provide a model for RNA binding by LigT, involving flexible loops lining the active site cavity. 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. Structural data [29] from these enzymes incidate that the 2 0 ,5 0 -adenosine bisphophate substrate binds along the opposite side of the active site, compared to LigT and CNPase (Fig 7A) . As the different structures predicted an RNA-binding surface on LigT, we further modeled a 3-residue RNA molecule with a terminal 2 0 -phosphate into the active site.	./cache/cord-002398-0a3okta0.txt	./txt/cord-002398-0a3okta0.txt