Recently the partial amino acid sequence of PARPSso helped us to get a new sight of its structural features, catalytic properties and correlation with PARP enzymes. The obtained results clearly indicate that the analyzed PARPSso N-terminus and tryptic peptides (about 60% of total residues) do not share structural similarity with any of known PARPs. A peculiar feature of N-terminus (30 residues) is that it contains an ATP-binding domain, with a characteristic Walker A motif, G-X-X-G-X-G-K-T/S.
A new sight of the ADP-ribosylation reaction in the thermophilic Crenarchaeon Sulfolobus solfataricus / DE MAIO, Anna; E., Porzio; Farina, Benedetta; FARAONE MENNELLA, MARIA ROSARIA. - ELETTRONICO. - (2008), pp. S5 P3-S5 P3. (Intervento presentato al convegno NAD2008 Meeting tenutosi a Hamburg (D) nel 14-17 settembre 2008).
A new sight of the ADP-ribosylation reaction in the thermophilic Crenarchaeon Sulfolobus solfataricus
DE MAIO, ANNA;FARINA, BENEDETTA;FARAONE MENNELLA, MARIA ROSARIA
2008
Abstract
Recently the partial amino acid sequence of PARPSso helped us to get a new sight of its structural features, catalytic properties and correlation with PARP enzymes. The obtained results clearly indicate that the analyzed PARPSso N-terminus and tryptic peptides (about 60% of total residues) do not share structural similarity with any of known PARPs. A peculiar feature of N-terminus (30 residues) is that it contains an ATP-binding domain, with a characteristic Walker A motif, G-X-X-G-X-G-K-T/S.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
