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Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.

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 (PfLipL1?243-279 ) 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. © 2017 Wiley Periodicals, Inc.

SUBMITTER: Guerra AJ

PROVIDER: S-EPMC5568926 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.

Guerra Alfredo J AJ Afanador Gustavo A GA Prigge Sean T ST

Proteins 20170607 9

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 (PfLipL1<sub>Δ243-279</sub> ) bound to lipoate, and validate the lipoylation activity of this construct in both an ...[more]

PMID: 28543853

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