Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.

2.50
Hdl Handle:
http://hdl.handle.net/10033/344385
Title:
Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.
Authors:
Singh, Bishal K; Sattler, Julia M; Chatterjee, Moon; Huttu, Jani; Schüler, Herwig; Kursula, Inari
Abstract:
Apicomplexan parasites, such as the malaria-causing Plasmodium, utilize an actin-based motor for motility and host cell invasion. The actin filaments of these parasites are unusually short, and actin polymerization is under strict control of a small set of regulatory proteins, which are poorly conserved with their mammalian orthologs. Actin depolymerization factors (ADFs) are among the most important actin regulators, affecting the rates of filament turnover in a multifaceted manner. Plasmodium has two ADFs that display low sequence homology with each other and with the higher eukaryotic family members. Here, we show that ADF2, like canonical ADF proteins but unlike ADF1, binds to both globular and filamentous actin, severing filaments and inducing nucleotide exchange on the actin monomer. The crystal structure of Plasmodium ADF1 shows major differences from the ADF consensus, explaining the lack of F-actin binding. Plasmodium ADF2 structurally resembles the canonical members of the ADF/cofilin family.
Citation:
Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite. 2011, 286 (32):28256-64 J. Biol. Chem.
Journal:
The Journal of biological chemistry
Issue Date:
12-Aug-2011
URI:
http://hdl.handle.net/10033/344385
DOI:
10.1074/jbc.M111.211730
PubMed ID:
21832095
Type:
Article
Language:
en
ISSN:
1083-351X
Appears in Collections:
publications of the research group CSSB

Full metadata record

DC FieldValue Language
dc.contributor.authorSingh, Bishal Ken
dc.contributor.authorSattler, Julia Men
dc.contributor.authorChatterjee, Moonen
dc.contributor.authorHuttu, Janien
dc.contributor.authorSchüler, Herwigen
dc.contributor.authorKursula, Inarien
dc.date.accessioned2015-02-12T13:11:48Z-
dc.date.available2015-02-12T13:11:48Z-
dc.date.issued2011-08-12-
dc.identifier.citationCrystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite. 2011, 286 (32):28256-64 J. Biol. Chem.en
dc.identifier.issn1083-351X-
dc.identifier.pmid21832095-
dc.identifier.doi10.1074/jbc.M111.211730-
dc.identifier.urihttp://hdl.handle.net/10033/344385-
dc.description.abstractApicomplexan parasites, such as the malaria-causing Plasmodium, utilize an actin-based motor for motility and host cell invasion. The actin filaments of these parasites are unusually short, and actin polymerization is under strict control of a small set of regulatory proteins, which are poorly conserved with their mammalian orthologs. Actin depolymerization factors (ADFs) are among the most important actin regulators, affecting the rates of filament turnover in a multifaceted manner. Plasmodium has two ADFs that display low sequence homology with each other and with the higher eukaryotic family members. Here, we show that ADF2, like canonical ADF proteins but unlike ADF1, binds to both globular and filamentous actin, severing filaments and inducing nucleotide exchange on the actin monomer. The crystal structure of Plasmodium ADF1 shows major differences from the ADF consensus, explaining the lack of F-actin binding. Plasmodium ADF2 structurally resembles the canonical members of the ADF/cofilin family.en
dc.language.isoenen
dc.subject.meshCrystallography, X-Rayen
dc.subject.meshDestrinen
dc.subject.meshPlasmodium bergheien
dc.subject.meshPlasmodium falciparumen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshProtozoan Proteinsen
dc.subject.meshSpecies Specificityen
dc.subject.meshStructure-Activity Relationshipen
dc.titleCrystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.en
dc.typeArticleen
dc.identifier.journalThe Journal of biological chemistryen

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