| Literature DB >> 28543853 |
Alfredo J Guerra1, Gustavo A Afanador1, Sean T Prigge1.
Abstract
Plasmodium falciparum lipoate protein ligase 1 (PfLipL1) is an ATP-dependent ligase that belongs to the biotin/lipoate A/B protein ligase family (PFAM PF03099). PfLipL1 is the only known canonical lipoate ligase in Pf and functions as a redox switch between two lipoylation routes in the parasite mitochondrion. Here, we report the crystal structure of a deletion construct of PfLipL1 (PfLipL1Δ243-279 ) bound to lipoate, and validate the lipoylation activity of this construct in both an in vitro lipoylation assay and a cell-based lipoylation assay. This characterization represents the first step in understanding the redox dependence of the lipoylation mechanism in malaria parasites. Proteins 2017; 85:1777-1783.Entities:
Keywords: LipL1; Plasmodium falciparum; lipoate; lipoate ligase; lipoylation; malaria
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Year: 2017 PMID: 28543853 PMCID: PMC5568926 DOI: 10.1002/prot.25324
Source DB: PubMed Journal: Proteins ISSN: 0887-3585