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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| Main Authors: | , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
[2010]
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| In: |
Acta crystallographica. Section F, Structural biology communications
Year: 2010, Volume: 66, Issue: 5, Pages: 583-587 |
| ISSN: | 2053-230X |
| DOI: | 10.1107/S1744309110011589 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1107/S1744309110011589 Verlag, lizenzpflichtig, Volltext: http://scripts.iucr.org/cgi-bin/paper?en5417 
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| Author Notes: | Jani Huttu, Bishal Kumar Singh, Saligram Prabhakar Bhargav, Julia M. Sattler, Herwig Schüler and Inari Kursula |
| Summary: | 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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| Item Description: | Gesehen am 02.06.2023 |
| Physical Description: | Online Resource |
| ISSN: | 2053-230X |
| DOI: | 10.1107/S1744309110011589 |