6TLB
Plasmodium falciparum lipocalin (PF3D7_0925900)
Summary for 6TLB
| Entry DOI | 10.2210/pdb6tlb/pdb |
| Descriptor | Serine/threonine protein kinase, GLYCEROL, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | lipocalin, malaria, infection, unknown function |
| Biological source | Plasmodium falciparum (isolate 3D7) |
| Total number of polymer chains | 4 |
| Total formula weight | 89402.13 |
| Authors | Burda, P.C.,Crosskey, T.D.,Lauk, K.,Wilmanns, M.,Gilberger, T.W. (deposition date: 2019-12-02, release date: 2020-06-24, Last modification date: 2024-11-06) |
| Primary citation | Burda, P.C.,Crosskey, T.,Lauk, K.,Zurborg, A.,Sohnchen, C.,Liffner, B.,Wilcke, L.,Pietsch, E.,Strauss, J.,Jeffries, C.M.,Svergun, D.I.,Wilson, D.W.,Wilmanns, M.,Gilberger, T.W. Structure-Based Identification and Functional Characterization of a Lipocalin in the Malaria Parasite Plasmodium falciparum. Cell Rep, 31:107817-107817, 2020 Cited by PubMed Abstract: Proteins of the lipocalin family are known to bind small hydrophobic ligands and are involved in various physiological processes ranging from lipid transport to oxidative stress responses. The genome of the malaria parasite Plasmodium falciparum contains a single protein PF3D7_0925900 with a lipocalin signature. Using crystallography and small-angle X-ray scattering, we show that the protein has a tetrameric structure of typical lipocalin monomers; hence we name it P. falciparum lipocalin (PfLCN). We show that PfLCN is expressed in the intraerythrocytic stages of the parasite and localizes to the parasitophorous and food vacuoles. Conditional knockdown of PfLCN impairs parasite development, which can be rescued by treatment with the radical scavenger Trolox or by temporal inhibition of hemoglobin digestion. This suggests a key function of PfLCN in counteracting oxidative stress-induced cell damage during multiplication of parasites within erythrocytes. PubMed: 32579913DOI: 10.1016/j.celrep.2020.107817 PDB entries with the same primary citation |
| Experimental method | SOLUTION SCATTERING X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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