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. 2019 Mar 5;10:394. doi: 10.3389/fmicb.2019.00394

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Copyright © 2019 Mishra, Singh and Singh.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Unique features of Plasmodium vivax SUB1 structure. Cartoon representation of overall structure of PvSUB1 (PDB: 4TR2). Overall structure comprises N-terminal insertion in prodomain comprising the “belt” domain (shown in yellow) followed by a classical bacterial-like prodomain (orange), and the C-terminal subtilisin-like catalytic domain (cyan). The catalytic triad (Asp316/His372/Ser549; Red/Gray/olive) is shown as spheres. The oxyanion hole residue (Asn464) is shown as blue sphere. Bound calcium ions are shown as green spheres. Out of four calcium binding sites, three (Ca1, Ca2, Ca3) are specific to parasite subtilases. Ca4 is conserved in all homologs of subtilisin. Bacillus subtilsin (PDB: 1SUP) is superimposed (shown in magenta) highlighting the unique insertions in parasite subtilases. All structure figures have been made in Pymol.