2F6I

Crystal structure of the ClpP protease catalytic domain from Plasmodium falciparum

Summary for 2F6I

• Entry DOI: 10.2210/pdb2f6i/pdb
• Descriptor: ATP-dependent CLP protease, putative (2 entities in total)
• Functional Keywords: clp protease, structural genomics, structural genomics consortium, sgc, hydrolase
• Biological source: Plasmodium falciparum (malaria parasite P. falciparum)
• Total number of polymer chains: 7
• Total formula weight: 174093.90

Authors

Mulichak, A.,Loppnau, P.,Bray, J.,Amani, M.,Vedadi, M.,Wasney, G.,Finerty, P.,Sundstrom, M.,Weigelt, J.,Edwards, A.,Arrowsmith, C.,Hui, R.,Plotnikova, O.,Structural Genomics Consortium (SGC) (deposition date: 2005-11-29, release date: 2005-12-20, Last modification date: 2023-08-23)

Primary citation

El Bakkouri, M.,Pow, A.,Mulichak, A.,Cheung, K.L.,Artz, J.D.,Amani, M.,Fell, S.,de Koning-Ward, T.F.,Goodman, C.D.,McFadden, G.I.,Ortega, J.,Hui, R.,Houry, W.A.
The Clp chaperones and proteases of the human malaria parasite Plasmodium falciparum.
J.Mol.Biol., 404:456-477, 2010

PubMed Abstract: The Clp chaperones and proteases play an important role in protein homeostasis in the cell. They are highly conserved across prokaryotes and found also in the mitochondria of eukaryotes and the chloroplasts of plants. They function mainly in the disaggregation, unfolding and degradation of native as well as misfolded proteins. Here, we provide a comprehensive analysis of the Clp chaperones and proteases in the human malaria parasite Plasmodium falciparum. The parasite contains four Clp ATPases, which we term PfClpB1, PfClpB2, PfClpC and PfClpM. One PfClpP, the proteolytic subunit, and one PfClpR, which is an inactive version of the protease, were also identified. Expression of all Clp chaperones and proteases was confirmed in blood-stage parasites. The proteins were localized to the apicoplast, a non-photosynthetic organelle that accommodates several important metabolic pathways in P. falciparum, with the exception of PfClpB2 (also known as Hsp101), which was found in the parasitophorous vacuole. Both PfClpP and PfClpR form mostly homoheptameric rings as observed by size-exclusion chromatography, analytical ultracentrifugation and electron microscopy. The X-ray structure of PfClpP showed the protein as a compacted tetradecamer similar to that observed for Streptococcus pneumoniae and Mycobacterium tuberculosis ClpPs. Our data suggest the presence of a ClpCRP complex in the apicoplast of P. falciparum.

PubMed: 20887733
DOI: 10.1016/j.jmb.2010.09.051

Experimental method

X-RAY DIFFRACTION (2.45 Å)