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. Author manuscript; available in PMC: 2014 Apr 2.
Published in final edited form as: Biochemistry. 2013 Mar 20;52(13):2309–2318. doi: 10.1021/bi300692g

Figure 3. CerADPr domain contains sequence and predicted structural conservation of other bacterial ADP-ribosyltransferases.

Figure 3

(A) A predicted structure-based alignment of the Cereus toxin ADPr domain (CerADPr) was generated with the crystal structure of Iota toxin ADP-ribosyltransferase domain Ia (PDB: 1GIR). Three regions of alignment that are common components of ADP-ribosyltransferase family members, including an Arg, the Ser-Thr-Ser motif, and the Gln/Glu-XXX-Glu sequence (“RSE” motif) are shown. The latter defines an active site glutamic acid that is conserved among ADP-ribosyltransferases. Secondary structure labeling is based off the Iota toxin Ia ADP-ribosyltransferase domain, starting with α-helix1 at residues 214–232. (B) CerADPr(E431D) ADP-ribosyltransferase activity was measured relative to CerADPr by incubation with Tx-100 HeLa cell lysate and 4 µM biotin-NAD for 1 hr at 25°C. The reaction mixture was processed as described in Figure 1 and the ADP-ribosylation of the high-molecular weight substrate is shown in the inset image.