Crystallization and preliminary structural characterization of the two actin-depolymerization factors of the malaria parasite
(2010) In Acta crystallographica. Section F, Structural biology communications 66(Pt 5). p.7-583- Abstract
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 A and belonged to space groups P3(1)21 or P3(2)21, with unit-cell parameters a = b = 68.8, c = 76.0 A, and P2(1)2(1)2, with unit-cell parameters a = 111.6, b = 57.9, c = 40.5 A, respectively, indicating the presence of one or... (More)
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 A and belonged to space groups P3(1)21 or P3(2)21, with unit-cell parameters a = b = 68.8, c = 76.0 A, and P2(1)2(1)2, with unit-cell parameters a = 111.6, b = 57.9, c = 40.5 A, respectively, indicating the presence of one or two molecules per asymmetric unit in both cases.
(Less)
- author
- Huttu, Jani
; Singh, Bishal Kumar
; Bhargav, Saligram Prabhakar
; Sattler, Julia M
; Schüler, Herwig
LU
and Kursula, Inari
- publishing date
- 2010-05-01
- type
- Contribution to journal
- publication status
- published
- keywords
- Crystallography, X-Ray, Models, Molecular, Plasmodium berghei/chemistry, Plasmodium falciparum/chemistry, Protozoan Proteins/chemistry
- in
- Acta crystallographica. Section F, Structural biology communications
- volume
- 66
- issue
- Pt 5
- pages
- 5 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:77952003787
- pmid:20445265
- ISSN
- 2053-230X
- DOI
- 10.1107/S1744309110011589
- language
- English
- LU publication?
- no
- id
- 52543420-0a61-45df-90c3-5d6c684c5cc0
- date added to LUP
- 2024-11-21 18:01:09
- date last changed
- 2025-03-28 16:24:54
@article{52543420-0a61-45df-90c3-5d6c684c5cc0, abstract = {{<p>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 A and belonged to space groups P3(1)21 or P3(2)21, with unit-cell parameters a = b = 68.8, c = 76.0 A, and P2(1)2(1)2, with unit-cell parameters a = 111.6, b = 57.9, c = 40.5 A, respectively, indicating the presence of one or two molecules per asymmetric unit in both cases.</p>}}, author = {{Huttu, Jani and Singh, Bishal Kumar and Bhargav, Saligram Prabhakar and Sattler, Julia M and Schüler, Herwig and Kursula, Inari}}, issn = {{2053-230X}}, keywords = {{Crystallography, X-Ray; Models, Molecular; Plasmodium berghei/chemistry; Plasmodium falciparum/chemistry; Protozoan Proteins/chemistry}}, language = {{eng}}, month = {{05}}, number = {{Pt 5}}, pages = {{7--583}}, publisher = {{John Wiley & Sons Inc.}}, series = {{Acta crystallographica. Section F, Structural biology communications}}, title = {{Crystallization and preliminary structural characterization of the two actin-depolymerization factors of the malaria parasite}}, url = {{http://dx.doi.org/10.1107/S1744309110011589}}, doi = {{10.1107/S1744309110011589}}, volume = {{66}}, year = {{2010}}, }