Open AccessCrystallization and preliminary structural characterization of the two actin‐depolymerization factors of the malaria parasite
Author(s) -
Huttu Jani,
Singh Bishal Kumar,
Bhargav Saligram Prabhakar,
Sattler Julia M.,
Schüler Herwig,
Kursula Inari
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110011589
Subject(s) - depolymerization , actin , plasmodium (life cycle) , crystallization , parasite hosting , biology , motility , microbiology and biotechnology , malaria , cytoskeleton , apicomplexa , plasmodium falciparum , biophysics , cell , biochemistry , chemistry , immunology , organic chemistry , world wide web , computer science
The malaria parasite Plasmodium depends on its actin‐based motor system for motility and host‐cell invasion. Actin‐depolymerization factors are important regulatory proteins that affect the rate of actin turnover. Plasmodium has two actin‐depolymerization factors which seem to have different functions and display low sequence homology to the higher eukaryotic family members. Plasmodium actin‐depolymerization factors 1 and 2 have been crystallized. The crystals diffracted X‐rays to maximum resolutions of 2.0 and 2.1 Å and belonged to space groups P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 68.8, c = 76.0 Å, and P 2 1 2 1 2, with unit‐cell parameters a = 111.6, b = 57.9, c = 40.5 Å, respectively, indicating the presence of one or two molecules per asymmetric unit in both cases.