NDLI: Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design.

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Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design.

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Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	AhYoung, Andrew P. Koehl, Antoine Cascio, Duilio Egea, Pascal F.
Description	Author Affiliation: AhYoung AP ( Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California.); Koehl A ( Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California.); Cascio D ( Department of Energy Institute for Genomics and Proteomics, UCLA, Los Angeles, California.); Egea PF ( Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California.)
Abstract	Caseinolytic chaperones and proteases (Clp) belong to the AAA+ protein superfamily and are part of the protein quality control machinery in cells. The eukaryotic parasite Plasmodium falciparum, the causative agent of malaria, has evolved an elaborate network of Clp proteins including two distinct ClpB ATPases. ClpB1 and ClpB2 are involved in different aspects of parasitic proteostasis. ClpB1 is present in the apicoplast, a parasite-specific and plastid-like organelle hosting various metabolic pathways necessary for parasite growth. ClpB2 localizes to the parasitophorous vacuole membrane where it drives protein export as core subunit of a parasite-derived protein secretion complex, the Plasmodium Translocon of Exported proteins (PTEX); this process is central to parasite virulence and survival in the human host. The functional associations of these two chaperones with parasite-specific metabolism and protein secretion make them prime drug targets. ClpB proteins function as unfoldases and disaggregases and share a common architecture consisting of four domains-a variable N-terminal domain that binds different protein substrates, followed by two highly conserved catalytic ATPase domains, and a C-terminal domain. Here, we report and compare the first crystal structures of the N terminal domains of ClpB1 and ClpB2 from Plasmodium and analyze their molecular surfaces. Solution scattering analysis of the N domain of ClpB2 shows that the average solution conformation is similar to the crystalline structure. These structures represent the first step towards the characterization of these two malarial chaperones and the reconstitution of the entire PTEX to aid structure-based design of novel anti-malarial drugs.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.2739
Journal	Protein Science
Issue Number	9
Volume Number	24
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2015-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphatases Chemistry Metabolism Antimalarials Plasmodium Falciparum Enzymology Protozoan Proteins Amino Acid Sequence Pharmacology Crystallography, X-ray Drug Design Models, Molecular Molecular Chaperones Molecular Sequence Data Molecular Targeted Therapy Genetics Protein Folding Protein Structure, Secondary Protein Transport Research Support, N.i.h., Extramural Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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