id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-348104-7662q8dg	Yang, Xiaoyun	Molecular basis for the MacroD1-mediated hydrolysis of ADP-ribosylation	2020-06-22		.txt	text/plain	4314	254	53	Taken together, our study provides structural and functional insights into the molecular mechanism of MacroD1-mediated ADPR hydrolysis and its role in DNA damage repair. Combining with our structural analysis and ADPR hydrolyzation assay, it suggests that distinct catalytic residues are responsible for the MacroD1-mediated ADPR hydrolysis, rather than the catalytic residues Asn 174 , Asp 184 and His 188 in the deacetylation of OAADPr. It is observed that Phe 272 adopts a significant conformational change in the catalytic pocket of MacroD1 upon ADPR binding, and that the corresponding phenyl group is evolutionarily conserved among macro domain hydrolases. In contrast, the structure of ADPR bound to the MacroH2A1.1 macro domain (inactive) reveals that the corresponding residue for MacroD1 Phe 272 is Asn 316 , and the disappearance of steric hindrance, which is generated by phenyl group, makes the distal ribose in a relatively extended conformation, in which its C1″ atom is far away from the catalytic water ( Fig. S3) (38) .	./cache/cord-348104-7662q8dg.txt	./txt/cord-348104-7662q8dg.txt