Figure 11

Conserved active site fold structure of the PARP domain. Fold-assisted AA alignments of the PARP catalytic core from (A) human PARP1 (HsPARP1), A. thaliana PARP-1 and -2 (AtPARP1, AtPARP2) and RCD1 (AtRCD1) and (B) A. thaliana RCD1 and SROs (AtSRO1-5). Consensus of conserved (*) and similar (: and .) AAs and conserved folds (α-helix or β-sheet) are indicated below the alignments. Additionally folds are shaded in the alignment with grey (α-helix) or yellow (β-sheet) backgrounds. Conserved ADP-ribosyl transferase catalytic triad, composed of three AAs at the C-terminus of β-sheet 1, middle of β-sheet 2 and N-terminal end of β-sheet 5, is indicated by turquoise background shading and an (‡) above the alignment. Alignments were performed with T-Coffee at EMBL-EBI http://www.ebi.ac.uk/Tools and hand-adjusted according to fold predictions performed with Psipred in the Phyre search [53]. AAs were color-coded according to their biochemical properties as in http://www.ebi.ac.uk/Tools/t-coffee/help.html#color.