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Figure 1
Unicellular pappalysin family members. Structure-assisted sequence alignment of selected pappalysins from prokaryotes and lower eukaryotes depicting the respective (potential) CDs and upstream PSs. The organism, the UniProt code plus the sequence identity with ulilysin in parentheses, and the organism category are displayed at the beginning of each sequence block, respectively. Very high, high and middle sequence similarities are characterized by magenta, green and yellow backgrounds, respectively. Regular secondary-structure elements (helices and strands as orange and blue bars, respectively) below and above the alignment correspond to ulilysin and (pro)mirolysin, respectively. Their numbering is consistent with that of ulilysin, see Tallant et al. (2006BB93). The conserved CG-motif responsible for latency in promirolysin is shown in bold. The number of additional N- and C-terminal residues is shown in parentheses. Residues not present in the structure of native promirolysin (this work; PDB entry 6r7v) and mature ulilysin (PDB entry 2cki) are denoted by grey bars above and below the alignment, respectively. The disulfides found in both ulilysin and mirolysin are shown as purple handles. Red scissors indicate autolytic activation points (P1′ residues) of ulilysin (Tallant et al., 2006BB93) and mirolysin (Koneru et al., 2017BB54).

IUCrJ
Volume 7| Part 1| January 2020| Pages 18-29
ISSN: 2052-2525
https://doi.org/10.1107/S2052252519013848