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Crystallization and preliminary structural characterization of the two actin-depolymerization factors of the malaria parasite

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 functio...

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Hauptverfasser: Huttu, Jani (VerfasserIn) , Singh, Bishal Kumar (VerfasserIn) , Bhargav, Saligram Prabhakar (VerfasserIn) , Sattler, Julia M. (VerfasserIn) , Schüler, Herwig (VerfasserIn) , Kursula, Inari (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: [2010]
In: Acta crystallographica. Section F, Structural biology communications
Year: 2010, Jahrgang: 66, Heft: 5, Pages: 583-587
ISSN:2053-230X
DOI:10.1107/S1744309110011589
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1107/S1744309110011589
Verlag, lizenzpflichtig, Volltext: http://scripts.iucr.org/cgi-bin/paper?en5417
Volltext
Verfasserangaben:Jani Huttu, Bishal Kumar Singh, Saligram Prabhakar Bhargav, Julia M. Sattler, Herwig Schüler and Inari Kursula

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520 |a 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 P3121 or P3221, with unit-cell parameters a = b = 68.8, c = 76.0 Å, and P21212, 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. 
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