Reche Gallardo, Pedro AntonioKoch-Nolte, FriedrichHaag, FriedrichBazan, Fernando2023-06-202023-06-2020011873-4863https://hdl.handle.net/20.500.14352/58250ADP-ribosyltransferases (ADPRTs) form an interesting class of enzymes with well-established roles as potent bacterial toxins and metabolic regulators. ADPRTs catalyze the transfer of the ADP-ribose moiety from NAD(+) onto specific substrates including proteins. ADP-ribosylation usually inactivates the function of the target. ADPRTs have become adapted to function in extra- and intracellular settings. Regulation of ADPRT activity can be mediated by ligand binding to associated regulatory domains, proteolytic cleavage, disulphide bond reduction, and association with other proteins. Crystallisation has revealed a conserved core set of elements that define an unusual minimal scaffold of the catalytic domain with remarkably plastic sequence requirements--only a single glutamic acid residue critical to catalytic activity is invariant. These inherent properties of ADPRTs suggest that the ADPRT catalytic fold is an attractive, malleable subject for protein design.engjournal articlehttp://www.elsevier.com/wps/find/journaldescription.cws_home/505515/description#descriptionopen accessADP-ribosylationBacterial toxinsAmino acid sequence alignmentSequence homologyStructure predictionProtein designEvoluciónBioinformáticaBiología molecular (Biología)2415 Biología Molecular