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5BWY

Structure of proplasmepsin II from Plasmodium falciparum, Space Group P43212

Summary for 5BWY
Entry DOI10.2210/pdb5bwy/pdb
DescriptorPlasmepsin-2 (2 entities in total)
Functional Keywordsmalaria, hydrolase
Biological sourcePlasmodium falciparum
Total number of polymer chains1
Total formula weight42374.97
Authors
Recacha, R.,Akopjana, I.,Tars, K.,Jaudzems, K. (deposition date: 2015-06-08, release date: 2015-12-16, Last modification date: 2024-11-06)
Primary citationRecacha, R.,Jaudzems, K.,Akopjana, I.,Jirgensons, A.,Tars, K.
Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins.
Acta Crystallogr F Struct Biol Commun, 72:659-666, 2016
Cited by
PubMed Abstract: 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.
PubMed: 27599854
DOI: 10.1107/S2053230X16011663
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.644 Å)
Structure validation

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