Crystal Structure of Plasmodium Falciparum Proplasmepsin IV: The Plasticity of Proplasmepsins

Acta Crystallographica Section F: Structural Biology and Crystallization Communications 2016
R. Recacha, Kristaps Jaudzems, I. Akopjana, Aigars Jirgensons, K. Tars

Plasmepsin IV from Plasmodium falciparum (PM IV) is a promising target for the development of novel antimalarial drugs. Here, the crystal structure of the truncated zymogen of PM IV (pPM IV), consisting of the mature enzyme plus a prosegment of 47 residues, has been determined at 1.5 Å resolution. pPM IV presents the fold previously described for studied proplasmepsins, displaying closer similarities to proplasmepin IV from P. vivax (pPvPM) than to the other two proplasmepsins from P. falciparum. The study and comparison of the pPM IV structure with the proplasmepsin structures described previously provide information about the similarities and differences in the inactivation-activation mechanisms among the plasmepsin zymogens.

Keywords
aspartic protease zymogen | malaria | Plasmodium falciparum | proplasmepsin IV
DOI
10.1107/S2053230X16011663
Hyperlink
http://scripts.iucr.org/cgi-bin/paper?S2053230X16011663

Recacha, R., Jaudzems, K., Akopjana, I., Jirgensons, A., Tars, K. Crystal Structure of Plasmodium Falciparum Proplasmepsin IV: The Plasticity of Proplasmepsins. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2016, Vol.72, pp.659-666. ISSN 2053-230X. Available from: doi:10.1107/S2053230X16011663

Publication language
English (en)