Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6TLB

Plasmodium falciparum lipocalin (PF3D7_0925900)

Summary for 6TLB
Entry DOI10.2210/pdb6tlb/pdb
DescriptorSerine/threonine protein kinase, GLYCEROL, SODIUM ION, ... (4 entities in total)
Functional Keywordslipocalin, malaria, infection, unknown function
Biological sourcePlasmodium falciparum (isolate 3D7)
Total number of polymer chains4
Total formula weight89402.13
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 citationBurda, 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: 32579913
DOI: 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

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon